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Volumn 9, Issue 2, 2010, Pages 197-212

Alpha-lactalbumin: Its production technologies and bioactive peptides

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA-LACTALBUMIN; ALPHA-LACTALBUMINS; AMYLOID FIBRIL; ANTI-TUMORS; APOPTOSIS; BIOACTIVE PEPTIDES; DRAWING STRATEGY; ENZYME HYDROLYSIS; FUNCTIONAL FOODS; GLOBULAR PROTEINS; INFANT FORMULA; MEMBRANE SEPARATION; MINERAL BINDING; PLANT PROTEASE; PRODUCTION TECHNOLOGY;

EID: 78649380209     PISSN: None     EISSN: 15414337     Source Type: Journal    
DOI: 10.1111/j.1541-4337.2009.00100.x     Document Type: Article
Times cited : (131)

References (122)
  • 1
    • 78649347483 scopus 로고    scopus 로고
    • Sequential separation of whey proteins and formulations thereof
    • inventors; Sepragen corporation, Hayward, assignee
    • Ahmed SH, Saxena V, Miranda QR, inventors; Sepragen corporation, Hayward, assignee. 1998. Sequential separation of whey proteins and formulations thereof. US Patent 5,756,680.
    • (1998) US Patent , vol.5 , pp. 756
    • Ahmed, S.H.1    Saxena, V.2    Miranda, Q.R.3
  • 2
    • 51249100844 scopus 로고    scopus 로고
    • Degradation of whey from caprine milk by human proteolytic enzymes, and the resulting antibacterial effect against Listeria monocytogenes
    • Almaas H, Berner V, Holm H, Langsrud T, Vegarud GE. 2008. Degradation of whey from caprine milk by human proteolytic enzymes, and the resulting antibacterial effect against Listeria monocytogenes. Small Rumin Res 79:11-5.
    • (2008) Small Rumin Res , vol.79 , pp. 11-15
    • Almaas, H.1    Berner, V.2    Holm, H.3    Langsrud, T.4    Vegarud, G.E.5
  • 4
    • 0028240897 scopus 로고
    • A new generation of information retrieval tools for biologists: the example of the expasy www Server
    • Appel RD, Bairoch A, Hochstrasser DF. 1994. A new generation of information retrieval tools for biologists: the example of the expasy www Server. Trends Biochem Sci 19:258-60.
    • (1994) Trends Biochem Sci , vol.19 , pp. 258-260
    • Appel, R.D.1    Bairoch, A.2    Hochstrasser, D.F.3
  • 5
    • 27444437672 scopus 로고    scopus 로고
    • Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy
    • Barbana C, Pérez MD, Sánchez L, Dalgalarrondo M, Chobert JM, Haertlé T, Calvo M. 2006. Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy. Int Dairy J 16:18-25.
    • (2006) Int Dairy J , vol.16 , pp. 18-25
    • Barbana, C.1    Pérez, M.D.2    Sánchez, L.3    Dalgalarrondo, M.4    Chobert, J.M.5    Haertlé, T.6    Calvo, M.7
  • 6
    • 0014964808 scopus 로고
    • Purification and properties of bovine milk glyco-α-lactalbumin
    • Barman TE. 1970. Purification and properties of bovine milk glyco-α-lactalbumin. Biochim Biophys Acta 214:242-4.
    • (1970) Biochim Biophys Acta , vol.214 , pp. 242-244
    • Barman, T.E.1
  • 8
    • 32444432050 scopus 로고    scopus 로고
    • Molecular characterization of peptides released from β-lactoglobulin and α-lactalbumin via cardosins A and B
    • Barros RM, Malcata FX. 2006. Molecular characterization of peptides released from β-lactoglobulin and α-lactalbumin via cardosins A and B. J Dairy Sci 89:483-94.
    • (2006) J Dairy Sci , vol.89 , pp. 483-494
    • Barros, R.M.1    Malcata, F.X.2
  • 9
    • 0002289064 scopus 로고
    • Binding of bivalent cations to α-lactalbumin and β-lactoglobulin: effect of pH and ionic strength
    • Baumy JJ, Brule G. 1988. Binding of bivalent cations to α-lactalbumin and β-lactoglobulin: effect of pH and ionic strength. Lait 68:33-48.
    • (1988) Lait , vol.68 , pp. 33-48
    • Baumy, J.J.1    Brule, G.2
  • 10
    • 41649092457 scopus 로고    scopus 로고
    • Antioxidant activity of whey protein fractions isolated by gel exclusion chromatography and protease treatment
    • Bayram T, Pekmez M, Arda N, Yalçin AS. 2008. Antioxidant activity of whey protein fractions isolated by gel exclusion chromatography and protease treatment. Talanta 75:705-9.
    • (2008) Talanta , vol.75 , pp. 705-709
    • Bayram, T.1    Pekmez, M.2    Arda, N.3    Yalçin, A.S.4
  • 12
    • 0023176333 scopus 로고
    • Immunostimulating properties and three-dimensional structure of two tripeptides from human and cow caseins
    • Berthou J, Migliore-Samour D, Lifchitz A, Delettre J, Floch F, Jollès P. 1987. Immunostimulating properties and three-dimensional structure of two tripeptides from human and cow caseins. FEBS Lett 218:55-8.
    • (1987) FEBS Lett , vol.218 , pp. 55-58
    • Berthou, J.1    Migliore-Samour, D.2    Lifchitz, A.3    Delettre, J.4    Floch, F.5    Jollès, P.6
  • 15
    • 0038175547 scopus 로고    scopus 로고
    • A novel antioxidant and antiapoptotic role of omeprazole to block gastric ulcer through scavenging of hydroxyl radical
    • Biswas K, Bandyopadhyay U, Chattopadhyay I, Varadaraj A, Ali E, Banerjee RK. 2003. A novel antioxidant and antiapoptotic role of omeprazole to block gastric ulcer through scavenging of hydroxyl radical. J Biol Chem 278:10993-1001.
    • (2003) J Biol Chem , vol.278 , pp. 10993-11001
    • Biswas, K.1    Bandyopadhyay, U.2    Chattopadhyay, I.3    Varadaraj, A.4    Ali, E.5    Banerjee, R.K.6
  • 16
    • 0035979766 scopus 로고    scopus 로고
    • Identification and quantification of major bovine milk proteins by liquid chromatography
    • Bordin G, Cordeiro Raposo F, de la Calle B, Rodriguez AR. 2001. Identification and quantification of major bovine milk proteins by liquid chromatography. J Chromatogr A 928:63-76.
    • (2001) J Chromatogr A , vol.928 , pp. 63-76
    • Bordin, G.1    Cordeiro Raposo, F.2    de la Calle, B.3    Rodriguez, A.R.4
  • 18
    • 0020459343 scopus 로고
    • Influence of dietary proteins on the immune system of mice
    • Bounous G, Kongshavn P. 1982. Influence of dietary proteins on the immune system of mice. J Nutr 112:1747-55.
    • (1982) J Nutr , vol.112 , pp. 1747-1755
    • Bounous, G.1    Kongshavn, P.2
  • 19
    • 0000794559 scopus 로고    scopus 로고
    • Optimisation of a whey protein fractionation process based on the selective precipitation of α-lactalbumin
    • Bramaud C, Aimar P, Daufin G. 1997. Optimisation of a whey protein fractionation process based on the selective precipitation of α-lactalbumin. Lait 77:411-23.
    • (1997) Lait , vol.77 , pp. 411-423
    • Bramaud, C.1    Aimar, P.2    Daufin, G.3
  • 21
    • 0038377201 scopus 로고    scopus 로고
    • Separation of α-lactalbumin and β-lactoglobulin using membrane ultrafiltration
    • Cheang B, Zydney AL. 2003. Separation of α-lactalbumin and β-lactoglobulin using membrane ultrafiltration. Biotechnol Bio Eng 83:201-9.
    • (2003) Biotechnol Bio Eng , vol.83 , pp. 201-209
    • Cheang, B.1    Zydney, A.L.2
  • 22
    • 34548634293 scopus 로고    scopus 로고
    • Use of macroporous adsorption resin for simultaneous desalting and debittering of whey protein hydrolysates
    • Cheison SC, Wang Z, Xu SY. 2007. Use of macroporous adsorption resin for simultaneous desalting and debittering of whey protein hydrolysates. Int J Food Sci Technol 42:1228-39.
    • (2007) Int J Food Sci Technol , vol.42 , pp. 1228-1239
    • Cheison, S.C.1    Wang, Z.2    Xu, S.Y.3
  • 23
    • 11144235692 scopus 로고    scopus 로고
    • A comparative study of the α-subdomains of bovine and human α-lactalbumin reveals key differences that correlate with molten globule stability
    • Chowdrury FA, Raleigh DP. 2005. A comparative study of the α-subdomains of bovine and human α-lactalbumin reveals key differences that correlate with molten globule stability. Protein Sci 14:89-96.
    • (2005) Protein Sci , vol.14 , pp. 89-96
    • Chowdrury, F.A.1    Raleigh, D.P.2
  • 24
    • 23744468294 scopus 로고    scopus 로고
    • Concentration of α-lactalbumin from cow milk whey through expanded bed adsorption using a hydrophobic resin
    • Conrado LS, Veredas V, Nóbrega ES, Santana CC. 2005. Concentration of α-lactalbumin from cow milk whey through expanded bed adsorption using a hydrophobic resin. Braz J Chem Eng 22:501-9.
    • (2005) Braz J Chem Eng , vol.22 , pp. 501-509
    • Conrado, L.S.1    Veredas, V.2    Nóbrega, E.S.3    Santana, C.C.4
  • 25
    • 0036891687 scopus 로고    scopus 로고
    • Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis
    • De-Laureto PP, Frare E, Gottardo R, Dael HV, Fontana A. 2002. Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis. Protein Sci 11:2932-46.
    • (2002) Protein Sci , vol.11 , pp. 2932-2946
    • De-Laureto, P.P.1    Frare, E.2    Gottardo, R.3    Dael, H.V.4    Fontana, A.5
  • 26
    • 33747501826 scopus 로고    scopus 로고
    • Preparation of angiotensin-I-converting enzyme inhibitory hydrolysates from unsupplemented caprine whey fermentation by various cheese microflora
    • Didelot S, Bordenave-Juchereau S, Rosenfeld E, Fruitier-Arnaudin I, Piot JM, Sannier F. 2006. Preparation of angiotensin-I-converting enzyme inhibitory hydrolysates from unsupplemented caprine whey fermentation by various cheese microflora. Int Dairy J 16:976-83.
    • (2006) Int Dairy J , vol.16 , pp. 976-983
    • Didelot, S.1    Bordenave-Juchereau, S.2    Rosenfeld, E.3    Fruitier-Arnaudin, I.4    Piot, J.M.5    Sannier, F.6
  • 28
    • 0142134260 scopus 로고    scopus 로고
    • Casein-derived bioactive phosphopeptides: role of phosphorylation and primary structure in promoting calcium uptake by HT-29 tumor cells
    • Ferraretto A, Gravaghi C, Fiorilli A, Tettamanti G. 2003. Casein-derived bioactive phosphopeptides: role of phosphorylation and primary structure in promoting calcium uptake by HT-29 tumor cells. FEBS Lett 551:92-8.
    • (2003) FEBS Lett , vol.551 , pp. 92-98
    • Ferraretto, A.1    Gravaghi, C.2    Fiorilli, A.3    Tettamanti, G.4
  • 29
    • 33748312144 scopus 로고    scopus 로고
    • Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins
    • Gauthier SF, Pouliot Y, Saint-Sauveur D. 2006. Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. Int Dairy J 16:1315-23.
    • (2006) Int Dairy J , vol.16 , pp. 1315-1323
    • Gauthier, S.F.1    Pouliot, Y.2    Saint-Sauveur, D.3
  • 30
    • 33646468916 scopus 로고    scopus 로고
    • Unique milk protein-based nanotubes: food and nanotechnology meet
    • Graveland-Bikker JF, De Kruif CG. 2006. Unique milk protein-based nanotubes: food and nanotechnology meet. Trends Food Sci Technol 17:196-203.
    • (2006) Trends Food Sci Technol , vol.17 , pp. 196-203
    • Graveland-Bikker, J.F.1    De Kruif, C.G.2
  • 31
    • 0029398314 scopus 로고
    • Susceptibility of β-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin
    • Guo MR, Fox PF, Flynn A. 1995. Susceptibility of β-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin. J Dairy Sci 78:2336-44.
    • (1995) J Dairy Sci , vol.78 , pp. 2336-2344
    • Guo, M.R.1    Fox, P.F.2    Flynn, A.3
  • 32
    • 68349125502 scopus 로고    scopus 로고
    • Crude goat whey fermentation by Kluyveromyces marxianus and Lactobacillus rhamnosus: contribution to proteolysis and ACE inhibitory activity
    • Hammea V, Sanniera F, Piota JM, Didelota S, Bordenave-Juchereaua S. 2009. Crude goat whey fermentation by Kluyveromyces marxianus and Lactobacillus rhamnosus: contribution to proteolysis and ACE inhibitory activity. J Dairy Res 76:152-7.
    • (2009) J Dairy Res , vol.76 , pp. 152-157
    • Hammea, V.1    Sanniera, F.2    Piota, J.M.3    Didelota, S.4    Bordenave-Juchereaua, S.5
  • 33
    • 41749086156 scopus 로고    scopus 로고
    • Antihypertensive and antimicrobial bioactive peptides from milk proteins
    • Haque E, Chand R. 2008. Antihypertensive and antimicrobial bioactive peptides from milk proteins. Eur Food Res Technol 227:7-15.
    • (2008) Eur Food Res Technol , vol.227 , pp. 7-15
    • Haque, E.1    Chand, R.2
  • 35
    • 34248366062 scopus 로고    scopus 로고
    • Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part 1: overview
    • Hayes M, Ross RP, Fitzgerard GF, Stanton C. 2007. Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part 1: overview. Biotechnol J 2:426-34.
    • (2007) Biotechnol J , vol.2 , pp. 426-434
    • Hayes, M.1    Ross, R.P.2    Fitzgerard, G.F.3    Stanton, C.4
  • 36
    • 13244277961 scopus 로고    scopus 로고
    • Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin Identification of active peptides by HPLC-MS
    • Hernández-Ledesma B, Valos AD, Bartolomé B, Amigo L. 2005. Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS. J Agric Food Chem 53:588-93.
    • (2005) J Agric Food Chem , vol.53 , pp. 588-593
    • Hernández-Ledesma, B.1    Valos, A.D.2    Bartolomé, B.3    Amigo, L.4
  • 39
    • 54149112723 scopus 로고    scopus 로고
    • Development and application of an optical biosensor immunoassay for α-lactalbumin in bovine milk
    • Indyk HE. 2009. Development and application of an optical biosensor immunoassay for α-lactalbumin in bovine milk. Int Dairy J 19:36-42.
    • (2009) Int Dairy J , vol.19 , pp. 36-42
    • Indyk, H.E.1
  • 40
    • 34648834587 scopus 로고    scopus 로고
    • Self-assembly of partially hydrolysed α-lactalbumin
    • Ipsen R, Otte J. 2007. Self-assembly of partially hydrolysed α-lactalbumin. Biotech Adv 25:602-5.
    • (2007) Biotech Adv , vol.25 , pp. 602-605
    • Ipsen, R.1    Otte, J.2
  • 41
    • 0027054727 scopus 로고
    • Specific binding sites on human phagocytic blood cells for Gly-Leu-Phe and Val-Glu-Pro-Ile-Pro-Tyr, immunostimulating peptides from human milk proteins
    • Jaziri M, Migliore SD, Casabianca MRP, Keddad K, Morgat JL, Jolles P. 1992. Specific binding sites on human phagocytic blood cells for Gly-Leu-Phe and Val-Glu-Pro-Ile-Pro-Tyr, immunostimulating peptides from human milk proteins. Biochim Biophys Acta 1160:251-61.
    • (1992) Biochim Biophys Acta , vol.1160 , pp. 251-261
    • Jaziri, M.1    Migliore, S.D.2    Casabianca, M.R.P.3    Keddad, K.4    Morgat, J.L.5    Jolles, P.6
  • 42
    • 0028331319 scopus 로고
    • Defensins: a family of antimicrobial and cytotoxic peptides
    • Kagan BL, Ganz T, Lehrer RI. 1994. Defensins: a family of antimicrobial and cytotoxic peptides. Toxicol 87:131-49.
    • (1994) Toxicol , vol.87 , pp. 131-149
    • Kagan, B.L.1    Ganz, T.2    Lehrer, R.I.3
  • 44
    • 34547476683 scopus 로고    scopus 로고
    • Growth-active peptides are produced from α-lactalbumin and lysozyme
    • Kanda Y, Hisayasu S, Abe Y, Katsura K, Mashimo K. 2007. Growth-active peptides are produced from α-lactalbumin and lysozyme. Life Sci 81:449-57.
    • (2007) Life Sci , vol.81 , pp. 449-457
    • Kanda, Y.1    Hisayasu, S.2    Abe, Y.3    Katsura, K.4    Mashimo, K.5
  • 45
    • 0029924099 scopus 로고    scopus 로고
    • Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins
    • Kayser H, Meisel H. 1996. Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Lett 383:18-20.
    • (1996) FEBS Lett , vol.383 , pp. 18-20
    • Kayser, H.1    Meisel, H.2
  • 46
    • 34848867314 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of heated whey: Iron-binding ability of peptides and antigenic protein fractions
    • Kim SB, Seo IS, Khan MA, Ki KS, Lee WS, Lee HJ, Shin HS, Kim HS. 2007. Enzymatic hydrolysis of heated whey: Iron-binding ability of peptides and antigenic protein fractions. J Dairy Sci 90:4033-42.
    • (2007) J Dairy Sci , vol.90 , pp. 4033-4042
    • Kim, S.B.1    Seo, I.S.2    Khan, M.A.3    Ki, K.S.4    Lee, W.S.5    Lee, H.J.6    Shin, H.S.7    Kim, H.S.8
  • 47
    • 20444415277 scopus 로고    scopus 로고
    • Unsaturated fatty acids induce cytotoxic aggregate formation of amyotrophic lateral sclerosis-linked superoxide dismutase 1 mutants
    • Kim YJ, Nakatomi R, Akagi T, Hashikawa T, Takahashi R. 2005. Unsaturated fatty acids induce cytotoxic aggregate formation of amyotrophic lateral sclerosis-linked superoxide dismutase 1 mutants. J Biol Chem 280:21515-21.
    • (2005) J Biol Chem , vol.280 , pp. 21515-21521
    • Kim, Y.J.1    Nakatomi, R.2    Akagi, T.3    Hashikawa, T.4    Takahashi, R.5
  • 49
    • 0019190922 scopus 로고
    • Effects of long-term blockade of angiotensin-converting enzyme with captopril (SQ14 225) on hemodynamics and circulating blood volume in SHR
    • Koike H, Ito K, Miyamoto M, Nishino H. 1980. Effects of long-term blockade of angiotensin-converting enzyme with captopril (SQ14,225) on hemodynamics and circulating blood volume in SHR. Hypertension 2:299-303.
    • (1980) Hypertension , vol.2 , pp. 299-303
    • Koike, H.1    Ito, K.2    Miyamoto, M.3    Nishino, H.4
  • 50
    • 36248946633 scopus 로고    scopus 로고
    • A new method for isolation of native α-lactalbumin from sweet whey
    • Konrad G, Kleinschmidt T. 2008. A new method for isolation of native α-lactalbumin from sweet whey. Int Dairy J 18:47-54.
    • (2008) Int Dairy J , vol.18 , pp. 47-54
    • Konrad, G.1    Kleinschmidt, T.2
  • 53
    • 33846811660 scopus 로고    scopus 로고
    • Effect of a milk drink supplemented with whey peptides on blood pressure in patients with mild hypertension
    • Lee YM, Skurk T, Hennig M, Hauner H. 2007. Effect of a milk drink supplemented with whey peptides on blood pressure in patients with mild hypertension. Eur J Nutr 46:21-7.
    • (2007) Eur J Nutr , vol.46 , pp. 21-27
    • Lee, Y.M.1    Skurk, T.2    Hennig, M.3    Hauner, H.4
  • 54
    • 84879485812 scopus 로고    scopus 로고
    • inventor; Wisconsin Alumni Research Foundation, assignee. US Patent 7,141,171,B2.
    • Lightfoot EN, inventor; Wisconsin Alumni Research Foundation, assignee. 2006. Membrane cascade-based separation. US Patent 7,141,171,B2.
    • (2006) Membrane cascade-based separation , vol.7 , pp. 141
    • Lightfoot, E.N.1
  • 55
    • 0141992791 scopus 로고    scopus 로고
    • Nutritional and physiologic significance of α-lactalbumin in infants
    • Lönnerdal B, Lien EL. 2003. Nutritional and physiologic significance of α-lactalbumin in infants. Nutr Rev 61:295-305.
    • (2003) Nutr Rev , vol.61 , pp. 295-305
    • Lönnerdal, B.1    Lien, E.L.2
  • 56
    • 84934444070 scopus 로고    scopus 로고
    • Protective effect of milk peptides: antibacterial and antitumor properties
    • López-Expósito I, Recio I. 2008. Protective effect of milk peptides: antibacterial and antitumor properties. Adv Exp Med Biol 606:271-93.
    • (2008) Adv Exp Med Biol , vol.606 , pp. 271-293
    • López-Expósito, I.1    Recio, I.2
  • 57
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • López-Fandiño R, Otte J, van Camp J. 2006. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int Dairy J 16:1277-93.
    • (2006) Int Dairy J , vol.16 , pp. 1277-1293
    • López-Fandiño, R.1    Otte, J.2    van Camp, J.3
  • 58
    • 0032538091 scopus 로고    scopus 로고
    • Extraction of α-lactalbumin from whey protein concentrate with modified inorganic membranes
    • Lucas D, Rabiller-Baudry M, Millesime L, Chaufer B, Daufin G. 1998. Extraction of α-lactalbumin from whey protein concentrate with modified inorganic membranes. J Membr Sci 148:1-12.
    • (1998) J Membr Sci , vol.148 , pp. 1-12
    • Lucas, D.1    Rabiller-Baudry, M.2    Millesime, L.3    Chaufer, B.4    Daufin, G.5
  • 59
    • 0022307525 scopus 로고
    • Rapid separation of milk whey proteins by anion exchange chromatography
    • Manji B, Hill A, Kakuda Y, Irvine DM. 1985. Rapid separation of milk whey proteins by anion exchange chromatography. J Dairy Sci 68:3176-9.
    • (1985) J Dairy Sci , vol.68 , pp. 3176-3179
    • Manji, B.1    Hill, A.2    Kakuda, Y.3    Irvine, D.M.4
  • 60
    • 20544471693 scopus 로고    scopus 로고
    • Evening intake of α-lactalbumin increases plasma tryptophan availability and improves morning alertness and brain measures of attention
    • Markus CR, Jonkman LM, Lammers JHC, Deutz NEP, Messer MH, Rigtering N. 2005. Evening intake of α-lactalbumin increases plasma tryptophan availability and improves morning alertness and brain measures of attention. J Clin Nutr 81:1026-33.
    • (2005) J Clin Nutr , vol.81 , pp. 1026-1033
    • Markus, C.R.1    Jonkman, L.M.2    Lammers, J.H.C.3    Deutz, N.E.P.4    Messer, M.H.5    Rigtering, N.6
  • 61
    • 0034085615 scopus 로고    scopus 로고
    • The bovine protein {alpha}-lactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress
    • Markus CR, Olivier B, Panhuysen GEM, Van Der Gugten J, Alles MS, Tuiten A, Westen-berg HGM, Fekkes D, Koppeschaar HF, De Haan E. 2000. The bovine protein {alpha}-lactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress. Am J Clin Nutr 71:1536-44.
    • (2000) Am J Clin Nutr , vol.71 , pp. 1536-1544
    • Markus, C.R.1    Olivier, B.2    Panhuysen, G.E.M.3    Van Der Gugten, J.4    Alles, M.S.5    Tuiten, A.6    Westen-berg, H.G.M.7    Fekkes, D.8    Koppeschaar, H.F.9    De Haan, E.10
  • 62
    • 3042686006 scopus 로고    scopus 로고
    • Therapeutic applications of whey protein
    • Marshall K. 2004. Therapeutic applications of whey protein. Altern Med Rev 9:136-56.
    • (2004) Altern Med Rev , vol.9 , pp. 136-156
    • Marshall, K.1
  • 63
    • 41849105252 scopus 로고    scopus 로고
    • Lipid-based colloidal carriers for peptide and protein delivery-liposomes versus lipid nanoparticles
    • Martins S, Sarmento B, Ferreira DC, Souto EB. 2007. Lipid-based colloidal carriers for peptide and protein delivery-liposomes versus lipid nanoparticles. Int J Nanomedicine 2:595-607.
    • (2007) Int J Nanomedicine , vol.2 , pp. 595-607
    • Martins, S.1    Sarmento, B.2    Ferreira, D.C.3    Souto, E.B.4
  • 64
    • 22544468502 scopus 로고    scopus 로고
    • Biochemical properties of peptides encrypted in bovine milk proteins
    • Meisel H. 2005. Biochemical properties of peptides encrypted in bovine milk proteins. Curr Med Chem 12:1905-19.
    • (2005) Curr Med Chem , vol.12 , pp. 1905-1919
    • Meisel, H.1
  • 66
    • 45849147682 scopus 로고    scopus 로고
    • Bioactive peptides and proteins from foods: indication for health effects
    • Möller N, Scholz-Ahrens K, Roos N, Schrezenmeir J. 2008. Bioactive peptides and proteins from foods: indication for health effects. Eur J Nutr 47:171-82.
    • (2008) Eur J Nutr , vol.47 , pp. 171-182
    • Möller, N.1    Scholz-Ahrens, K.2    Roos, N.3    Schrezenmeir, J.4
  • 67
    • 29744451337 scopus 로고    scopus 로고
    • Phospholipids interactions protect the milk allergen α-lactalbumin from proteolysis during in vitro digestion
    • Moreno FJ, Mackie AR, Mills ENC. 2005. Phospholipids interactions protect the milk allergen α-lactalbumin from proteolysis during in vitro digestion. J Agric Food Chem 53:9810-6.
    • (2005) J Agric Food Chem , vol.53 , pp. 9810-9816
    • Moreno, F.J.1    Mackie, A.R.2    Mills, E.N.C.3
  • 68
    • 0029937138 scopus 로고    scopus 로고
    • Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme in-hibitory activity
    • Mullally MM, Meisel H, FitzGerald RJ. 1996. Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme in-hibitory activity. Biol Chem Hoppe-Seyler 377:259-60.
    • (1996) Biol Chem Hoppe-Seyler , vol.377 , pp. 259-260
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 69
    • 0031464182 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins
    • Mullally MM, Meisel H, FitzGerald RJ. 1997. Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins. Int Dairy J 7:299-303.
    • (1997) Int Dairy J , vol.7 , pp. 299-303
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 70
    • 0344946472 scopus 로고    scopus 로고
    • Purification of α-lactalbumin from a prepurified acid whey: ultrafiltration or precipitation
    • Muller A, Chaufer B, Merin U, Daufin G. 2003. Purification of α-lactalbumin from a prepurified acid whey: ultrafiltration or precipitation. Lait 83:439-51.
    • (2003) Lait , vol.83 , pp. 439-451
    • Muller, A.1    Chaufer, B.2    Merin, U.3    Daufin, G.4
  • 71
    • 0033518550 scopus 로고    scopus 로고
    • Ultrafiltration modes of operation for the separation of α-lactalbumin from acid casein whey
    • Muller A, Daufin G, Chaufer B. 1999. Ultrafiltration modes of operation for the separation of α-lactalbumin from acid casein whey. J Membr Sci 153:9-21.
    • (1999) J Membr Sci , vol.153 , pp. 9-21
    • Muller, A.1    Daufin, G.2    Chaufer, B.3
  • 73
    • 0029365965 scopus 로고
    • Blocking of CD4 cell receptors for the human immunodeficiency virus type 1 (HIV-1) by chemically modified bovine milk proteins: potential for AIDS prophylaxis
    • Neurath AR, Debnath AK, Strick N, Li YY, Lin K, Jiang S. 1995. Blocking of CD4 cell receptors for the human immunodeficiency virus type 1 (HIV-1) by chemically modified bovine milk proteins: potential for AIDS prophylaxis. J Mol Recognit 8:304-16.
    • (1995) J Mol Recognit , vol.8 , pp. 304-316
    • Neurath, A.R.1    Debnath, A.K.2    Strick, N.3    Li, Y.Y.4    Lin, K.5    Jiang, S.6
  • 74
    • 0038128669 scopus 로고    scopus 로고
    • Isolation of α-lactalbumin, β-lactoglobulin, and bovine serum albumin from cow's milk using gel filtration and anion-exchange chromatography including evaluation of their antigenicity
    • Neyestani TR, Jalali M, Pezeshki M. 2003. Isolation of α-lactalbumin, β-lactoglobulin, and bovine serum albumin from cow's milk using gel filtration and anion-exchange chromatography including evaluation of their antigenicity. Protein Expr Purif 29:202-8.
    • (2003) Protein Expr Purif , vol.29 , pp. 202-208
    • Neyestani, T.R.1    Jalali, M.2    Pezeshki, M.3
  • 78
    • 0038121718 scopus 로고    scopus 로고
    • The antiviral activity of naturally occurring proteins and their peptide fragments after chemical modification
    • Oevermann A, Engels M, Thomas U, Pellegrini A. 2003. The antiviral activity of naturally occurring proteins and their peptide fragments after chemical modification. Antiviral Res 59:23-33.
    • (2003) Antiviral Res , vol.59 , pp. 23-33
    • Oevermann, A.1    Engels, M.2    Thomas, U.3    Pellegrini, A.4
  • 79
    • 0347626245 scopus 로고    scopus 로고
    • Alpha-lactalbuminenriched diets enhance serotonin release and induce anxiolytic and rewarding effects in the rat. Behav
    • Orosco M, Rouch C, Beslot F, Feurte S, Regnault A, Dauge V. 2004. Alpha-lactalbuminenriched diets enhance serotonin release and induce anxiolytic and rewarding effects in the rat. Behav Brain Res 148:1-10.
    • (2004) Brain Res , vol.148 , pp. 1-10
    • Orosco, M.1    Rouch, C.2    Beslot, F.3    Feurte, S.4    Regnault, A.5    Dauge, V.6
  • 80
    • 12344306647 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin
    • Otte J, Ipsen R, Bauer R, Bjerrum MJ, Waninge R. 2005. Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin. Int Dairy J 15:219-29.
    • (2005) Int Dairy J , vol.15 , pp. 219-229
    • Otte, J.1    Ipsen, R.2    Bauer, R.3    Bjerrum, M.J.4    Waninge, R.5
  • 81
    • 33846024711 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis
    • Otte J, Shalaby SM, Zakora M, Pripp AH, El-Shabrawy SA. 2007a. Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis. Int Dairy J 17:488-503.
    • (2007) Int Dairy J , vol.17 , pp. 488-503
    • Otte, J.1    Shalaby, S.M.2    Zakora, M.3    Pripp, A.H.4    El-Shabrawy, S.A.5
  • 82
    • 34548484135 scopus 로고    scopus 로고
    • Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis
    • Otte J, Shalaby SMA, Zakora M, Nielsen MS. 2007b. Fractionation and identification of ACE-inhibitory peptides from α-lactalbumin and β-casein produced by thermolysin-catalysed hydrolysis. Int Dairy J 17:1460-72.
    • (2007) Int Dairy J , vol.17 , pp. 1460-1472
    • Otte, J.1    Shalaby, S.M.A.2    Zakora, M.3    Nielsen, M.S.4
  • 83
    • 0033022708 scopus 로고    scopus 로고
    • Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule
    • Pellegrini A, Thomas U, Bramaz N, Hunziker P, Fellenberg RV. 1999. Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule. Biochim Biophys Acta 1426:439-48.
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 439-448
    • Pellegrini, A.1    Thomas, U.2    Bramaz, N.3    Hunziker, P.4    Fellenberg, R.V.5
  • 84
    • 0026560481 scopus 로고
    • Bactericidal activities of lysozyme and aprotinin against Gram-negative and Gram-positive bacteria related to their basic character
    • Pellegrini A, Thomas U, Fellenberg RV, Wild P. 1992. Bactericidal activities of lysozyme and aprotinin against Gram-negative and Gram-positive bacteria related to their basic character. J Appl Microbiol 72:180-7.
    • (1992) J Appl Microbiol , vol.72 , pp. 180-187
    • Pellegrini, A.1    Thomas, U.2    Fellenberg, R.V.3    Wild, P.4
  • 85
    • 0021979565 scopus 로고
    • Cation binding effects on the pH, thermal and urea denaturation transitions in α-lactalbumin
    • Permyakov EA, Morozova LA Burstein EA. 1985. Cation binding effects on the pH, thermal and urea denaturation transitions in α-lactalbumin. Biophys Chem 21:21-31.
    • (1985) Biophys Chem , vol.21 , pp. 21-31
    • Permyakov, E.A.1    Morozova, L.A.2    Burstein, E.A.3
  • 86
    • 2442575245 scopus 로고    scopus 로고
    • No need to be HAMLET or BAMLET to interact with histones: Binding of monomeric alpha-lactalbumin into histones and basic poly-amino acids
    • Permyakov SE, Pershikova IV, Khokhlova TI, Uversky VN, Permyakov EA. 2004. No need to be HAMLET or BAMLET to interact with histones: Binding of monomeric alpha-lactalbumin into histones and basic poly-amino acids. Biochemistry 43:5575-82.
    • (2004) Biochemistry , vol.43 , pp. 5575-5582
    • Permyakov, S.E.1    Pershikova, I.V.2    Khokhlova, T.I.3    Uversky, V.N.4    Permyakov, E.A.5
  • 87
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: opioid and ACE-inhibitory peptide
    • Pihlanto-Leppälä A. 2001. Bioactive peptides derived from bovine whey proteins: opioid and ACE-inhibitory peptide. Trends Food Sci Technol 11:347-56.
    • (2001) Trends Food Sci Technol , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 88
    • 0034141231 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory properties of whey protein digest: concentration and characterisation of active peptides
    • Pihlanto-Leppälä A, Koskinen P, Piilola K, Tupasela T, Korhonen H. 2000. Angiotensin I-converting enzyme inhibitory properties of whey protein digest: concentration and characterisation of active peptides. J Dairy Res 67:53-64.
    • (2000) J Dairy Res , vol.67 , pp. 53-64
    • Pihlanto-Leppälä, A.1    Koskinen, P.2    Piilola, K.3    Tupasela, T.4    Korhonen, H.5
  • 89
    • 0032717550 scopus 로고    scopus 로고
    • The effect of α-lactalbumin and β-lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103
    • Pihlanto-Leppälä A, Marnila P, Hubert L, Rokka T, Korhonen HJT, Karp M. 1999. The effect of α-lactalbumin and β-lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103. J Appl Microbiol 87:540-5.
    • (1999) J Appl Microbiol , vol.87 , pp. 540-545
    • Pihlanto-Leppälä, A.1    Marnila, P.2    Hubert, L.3    Rokka, T.4    Korhonen, H.J.T.5    Karp, M.6
  • 90
    • 33748319573 scopus 로고    scopus 로고
    • Antioxidative peptides derived from milk proteins
    • Pihlanto A. 2006. Antioxidative peptides derived from milk proteins. Int Dairy J 16:1306-14.
    • (2006) Int Dairy J , vol.16 , pp. 1306-1314
    • Pihlanto, A.1
  • 91
    • 0033801179 scopus 로고    scopus 로고
    • Hydrolysis of ovine, caprine and bovine whey proteins by trypsin and pepsin
    • Pintado ME, Malcata FX. 2000. Hydrolysis of ovine, caprine and bovine whey proteins by trypsin and pepsin. Bioprocess Biosyst Eng 23:275-82.
    • (2000) Bioprocess Biosyst Eng , vol.23 , pp. 275-282
    • Pintado, M.E.1    Malcata, F.X.2
  • 92
    • 0032911654 scopus 로고    scopus 로고
    • Fractionation of whey protein hydrolysates using charged UF/NF membranes
    • Pouliot Y, Wijers MC, Gauthier SF, Nadeau L. 1999. Fractionation of whey protein hydrolysates using charged UF/NF membranes. J Membr Sci 158:105-14.
    • (1999) J Membr Sci , vol.158 , pp. 105-114
    • Pouliot, Y.1    Wijers, M.C.2    Gauthier, S.F.3    Nadeau, L.4
  • 93
    • 85048228236 scopus 로고    scopus 로고
    • Effect of peptides derived from food proteins on blood pressure: a meta-analysis of randomized controlled trials
    • (10.3402/fnr.v52i0.1920)
    • Pripp H. 2008. Effect of peptides derived from food proteins on blood pressure: a meta-analysis of randomized controlled trials. Food Nutr Res 52:(10.3402/fnr.v52i0.1920).
    • (2008) Food Nutr Res , vol.52
    • Pripp, H.1
  • 94
    • 10444265979 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship modeling of ACE-inhibitory peptides derived from milk proteins
    • Pripp AH, Isaksson T, Stepaniak L, Sørhaug T. 2004. Quantitative structure-activity relationship modeling of ACE-inhibitory peptides derived from milk proteins. Eur Food Res Technol 219:579-83.
    • (2004) Eur Food Res Technol , vol.219 , pp. 579-583
    • Pripp, A.H.1    Isaksson, T.2    Stepaniak, L.3    Sørhaug, T.4
  • 95
    • 56449106674 scopus 로고    scopus 로고
    • Probing the effect of temperature on the backbone dynamics of the human α-lactalbumin molten globule
    • Ramboarina SP, Redfield C. 2008. Probing the effect of temperature on the backbone dynamics of the human α-lactalbumin molten globule. J Am Chem Soc 130:15318-26.
    • (2008) J Am Chem Soc , vol.130 , pp. 15318-15326
    • Ramboarina, S.P.1    Redfield, C.2
  • 96
    • 23844479241 scopus 로고    scopus 로고
    • Cationic liposome-microtubule complexes: Pathways to the formation of two-state lipid-protein nanotubes with open or closed ends
    • Raviv U, Needleman DJ, Li Y, Miller HP, Wilson L, Safinya CR. 2005. Cationic liposome-microtubule complexes: Pathways to the formation of two-state lipid-protein nanotubes with open or closed ends. Proc Natl Acad Sci USA 102:11167-72.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11167-11172
    • Raviv, U.1    Needleman, D.J.2    Li, Y.3    Miller, H.P.4    Wilson, L.5    Safinya, C.R.6
  • 98
    • 0034221181 scopus 로고    scopus 로고
    • Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese
    • Saito T, Nakamura T, Kitazawa H, Kawai Y, Itoh T. 2000. Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese. J Dairy Sci 83:1434-40.
    • (2000) J Dairy Sci , vol.83 , pp. 1434-1440
    • Saito, T.1    Nakamura, T.2    Kitazawa, H.3    Kawai, Y.4    Itoh, T.5
  • 99
    • 42249100527 scopus 로고    scopus 로고
    • Effects of α-lactalbumin-enriched formula containing different concentrations of glycomacropeptide on infant nutrition
    • Sandström O, Lönnerdal B, Graverholt G, Hernell O. 2008. Effects of α-lactalbumin-enriched formula containing different concentrations of glycomacropeptide on infant nutrition. Am J Clin Nutr 87:921-8.
    • (2008) Am J Clin Nutr , vol.87 , pp. 921-928
    • Sandström, O.1    Lönnerdal, B.2    Graverholt, G.3    Hernell, O.4
  • 100
    • 44649172609 scopus 로고    scopus 로고
    • Self-assembling peptide nanotubes
    • Scanlon S, Aggeli A. 2008. Self-assembling peptide nanotubes. Nanotoday 3:3-4.
    • (2008) Nanotoday , pp. 3-4
    • Scanlon, S.1    Aggeli, A.2
  • 102
    • 0028829497 scopus 로고
    • Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates
    • Schmidt DG, Meijer RJGM, Slangen CJ, Beresteijn ECH. 1995. Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates. Clin Exp Allergy 25:1007-17.
    • (1995) Clin Exp Allergy , vol.25 , pp. 1007-1017
    • Schmidt, D.G.1    Meijer, R.J.G.M.2    Slangen, C.J.3    Beresteijn, E.C.H.4
  • 103
    • 58849127006 scopus 로고    scopus 로고
    • Nanotechnology and its applications in the food sector
    • Sozer N, Kokini JL. 2009. Nanotechnology and its applications in the food sector. Trends Biotechnol 27:82-9.
    • (2009) Trends Biotechnol , vol.27 , pp. 82-89
    • Sozer, N.1    Kokini, J.L.2
  • 104
    • 0034101865 scopus 로고    scopus 로고
    • Isolation and characterization of free radical scavenging activities peptides derived from casein
    • Suetsuna K, Ukeda H, Ochi H. 2000. Isolation and characterization of free radical scavenging activities peptides derived from casein. J Nutr Biochem 11:128-31.
    • (2000) J Nutr Biochem , vol.11 , pp. 128-131
    • Suetsuna, K.1    Ukeda, H.2    Ochi, H.3
  • 107
    • 78649355366 scopus 로고    scopus 로고
    • Svenning C, Vegarud GE, editors., Wellington, New Zealand. IDF Nutrition Week
    • Svenning C, Vegarud GE, editors. Proceeding of dairy foods in health conference; 1998; Wellington, New Zealand. IDF Nutrition Week.
    • (1998) Proceeding of dairy foods in health conference
  • 109
    • 0036693736 scopus 로고    scopus 로고
    • Anti-hypertensive activity of fermented dairy products containing biogenic peptides
    • Takano DT. 2002. Anti-hypertensive activity of fermented dairy products containing biogenic peptides. Antonie van Leeuwenhoek 82:333-40.
    • (2002) Antonie van Leeuwenhoek , vol.82 , pp. 333-340
    • Takano, D.T.1
  • 110
    • 8344252020 scopus 로고    scopus 로고
    • Fractionation of whey proteins and caseinomacropeptide by means of enzymatic crosslinking and membrane separation techniques
    • Tolkach A, Kulozik U. 2005. Fractionation of whey proteins and caseinomacropeptide by means of enzymatic crosslinking and membrane separation techniques. J Food Eng 67:13-20.
    • (2005) J Food Eng , vol.67 , pp. 13-20
    • Tolkach, A.1    Kulozik, U.2
  • 111
    • 29544447014 scopus 로고    scopus 로고
    • Optimization of thermal pretreatment conditions for the separation of native α-lactalbumin from whey protein concentrates by means of selective denaturation of β-lactoglobulin
    • Tolkach A, Steinle S, Kulozik U. 2005. Optimization of thermal pretreatment conditions for the separation of native α-lactalbumin from whey protein concentrates by means of selective denaturation of β-lactoglobulin. J Food Sci 70:E557-66.
    • (2005) J Food Sci , vol.70
    • Tolkach, A.1    Steinle, S.2    Kulozik, U.3
  • 112
    • 34548324364 scopus 로고    scopus 로고
    • Antihypertensive effect of bioactive peptides produced by protease-facilitated lactic acid fermentation of milk
    • Tsai JS, Chen TJ, Pan BS, Gong SD, Chung MY. 2008. Antihypertensive effect of bioactive peptides produced by protease-facilitated lactic acid fermentation of milk. Food Chem 106:552-8.
    • (2008) Food Chem , vol.106 , pp. 552-558
    • Tsai, J.S.1    Chen, T.J.2    Pan, B.S.3    Gong, S.D.4    Chung, M.Y.5
  • 113
    • 23944460481 scopus 로고    scopus 로고
    • Anti-alopecia effect of Gly-Leu-Phe, an immunostimulating peptide derived from α-lactalbumin
    • Tsuruki T, Yoshikawa M. 2005. Anti-alopecia effect of Gly-Leu-Phe, an immunostimulating peptide derived from α-lactalbumin. Biosci Biotechnol Biochem 69:1633-5.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 1633-1635
    • Tsuruki, T.1    Yoshikawa, M.2
  • 114
    • 0034492053 scopus 로고    scopus 로고
    • Mineral-binding milk proteins and peptides: occurrence, biochemical and technological characteristics
    • Vegarud GE, Langsrud T, Svenning C. 2000. Mineral-binding milk proteins and peptides: occurrence, biochemical and technological characteristics. Br J Nutr 84:91-8.
    • (2000) Br J Nutr , vol.84 , pp. 91-98
    • Vegarud, G.E.1    Langsrud, T.2    Svenning, C.3
  • 115
    • 6944221879 scopus 로고    scopus 로고
    • Bioavailability of angiotensin I converting enzyme inhibitory peptides
    • Vermeirssen V, Camp JV, Verstraete W. 2004. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr 92:357-66.
    • (2004) Br J Nutr , vol.92 , pp. 357-366
    • Vermeirssen, V.1    Camp, J.V.2    Verstraete, W.3
  • 116
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benede GB, Condron MM, Teplow DB. 1997. Amyloid β-protein fibrillogenesis detection of a protofibrillar intermediate. J Biol Chem 272:22364-72.
    • (1997) J Biol Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benede, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 117
    • 0030025082 scopus 로고    scopus 로고
    • Disulfide determinants of calcium-induced packing in α-lactalbumin
    • Wu LC, Schulman BA, Peng ZY, Kim PS. 1996. Disulfide determinants of calcium-induced packing in α-lactalbumin. Biochemistry 35:859-63.
    • (1996) Biochemistry , vol.35 , pp. 859-863
    • Wu, L.C.1    Schulman, B.A.2    Peng, Z.Y.3    Kim, P.S.4
  • 119
    • 33747773827 scopus 로고    scopus 로고
    • Structural changes of α-lactalbumin induced by low PH and oleic acid
    • Yang F, Zhang M, Chen J, Liang Y. 2006. Structural changes of α-lactalbumin induced by low PH and oleic acid. Biochim Biophys Acta 1764:1389-96.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1389-1396
    • Yang, F.1    Zhang, M.2    Chen, J.3    Liang, Y.4
  • 120
    • 0347766076 scopus 로고    scopus 로고
    • The effects of shortening lactoferrin derived peptides against tumour cells, bacteria and normal human cells
    • Yang N, Strøm MB, Mekonnen SM, Svendsen JS, Rekdal Ø. 2004. The effects of shortening lactoferrin derived peptides against tumour cells, bacteria and normal human cells. J Peptide Sci 10:37-46.
    • (2004) J Peptide Sci , vol.10 , pp. 37-46
    • Yang, N.1    Strøm, M.B.2    Mekonnen, S.M.3    Svendsen, J.S.4    Rekdal, Ø.5
  • 121
    • 0034536951 scopus 로고    scopus 로고
    • Isolation of lactoperoxidase, lactoferrin, α-lactalbumin β-lactoglobulin B and β-lactoglobulin A from bovine rennet whey using ion exchange chromatography
    • Ye X, Yoshida S, Ng TB. 2000. Isolation of lactoperoxidase, lactoferrin, α-lactalbumin, β-lactoglobulin B and β-lactoglobulin A from bovine rennet whey using ion exchange chromatography. Int J Biochem Cell Biol 32:1143-50.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 1143-1150
    • Ye, X.1    Yoshida, S.2    Ng, T.B.3
  • 122
    • 67349213968 scopus 로고    scopus 로고
    • Cytotoxic aggregates of α-lactalbumin induced by unsaturated fatty acid induce apoptosis in tumor cells
    • Zhang M, Yang Jr F, Yang F, Chen J, Zheng CY, Liang Y. 2009. Cytotoxic aggregates of α-lactalbumin induced by unsaturated fatty acid induce apoptosis in tumor cells. Chem Biol Interact 180:131-42.
    • (2009) Chem Biol Interact , vol.180 , pp. 131-142
    • Zhang, M.1    Yang F., Jr.2    Yang, F.3    Chen, J.4    Zheng, C.Y.5    Liang, Y.6


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