메뉴 건너뛰기




Volumn 57, Issue 2-3, 2004, Pages 173-188

Angiotensin I-converting-enzyme-inhibitory and antimicrobial bioactive peptides

Author keywords

ACE inhibitory peptides; Antimicrobial peptides; Bioactive peptides; Lactic acid bacteria; Lactobacillus helveticus; Milk proteins

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; MILK PROTEIN; PEPTIDE;

EID: 2442700132     PISSN: 1364727X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-0307.2004.00139.x     Document Type: Conference Paper
Times cited : (225)

References (101)
  • 1
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger B (1997) Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. Journal of Membrane Biology 156 197-211.
    • (1997) Journal of Membrane Biology , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 3
    • 0033962437 scopus 로고    scopus 로고
    • Post-translational phosphorylation affects the IgE binding activity of caseins
    • Bernard H, Meisel H, Creminon C and Wal J M (2000) Post-translational phosphorylation affects the IgE binding activity of caseins. FEBS Letters 467 239-244.
    • (2000) FEBS Letters , vol.467 , pp. 239-244
    • Bernard, H.1    Meisel, H.2    Creminon, C.3    Wal, J.M.4
  • 4
    • 0033863173 scopus 로고    scopus 로고
    • Combinatorial libraries: A tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies
    • Blondelle S E and Lohner K (2000) Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies. Biopolymers 55 74-87.
    • (2000) Biopolymers , vol.55 , pp. 74-87
    • Blondelle, S.E.1    Lohner, K.2
  • 6
    • 0027976788 scopus 로고
    • Glutamine and the immune system
    • Calder P C (1994) Glutamine and the immune system. Clinical Nutrition 13 2-8.
    • (1994) Clinical Nutrition , vol.13 , pp. 2-8
    • Calder, P.C.1
  • 9
    • 0001981775 scopus 로고
    • Biologically functional peptides from food proteins: New opioid peptides from milk proteins
    • Feeney R E and Whitaker J, eds. New York: Marcel Dekker
    • Chiba H and Yoshikawa M (1986) Biologically functional peptides from food proteins: new opioid peptides from milk proteins. In Protein Tailoring for Food and Medical Uses, pp 123-153. Feeney R E and Whitaker J, eds. New York: Marcel Dekker.
    • (1986) Protein Tailoring for Food and Medical Uses , pp. 123-153
    • Chiba, H.1    Yoshikawa, M.2
  • 10
    • 0000022216 scopus 로고
    • Bioactive peptides derived from food proteins
    • Chiba H and Yoshikawa M (1991) Bioactive peptides derived from food proteins. Kagaku to Seibutsu 29 454-458.
    • (1991) Kagaku to Seibutsu , vol.29 , pp. 454-458
    • Chiba, H.1    Yoshikawa, M.2
  • 11
    • 0024372610 scopus 로고
    • Opioid antagonist peptides derived from kappa-casein
    • Chiba H, Tani F and Yoshikawa M (1989) Opioid antagonist peptides derived from kappa-casein. Journal of Dairy Research 56 363-366.
    • (1989) Journal of Dairy Research , vol.56 , pp. 363-366
    • Chiba, H.1    Tani, F.2    Yoshikawa, M.3
  • 13
    • 0026652726 scopus 로고
    • Identification of C-terminal peptides of bovine β-casein that enhance proliferation of rat lymphocytes
    • Coste M, Rochet V, Lèonil J, Mollè D, Bouhallab S and Tomè D (1992) Identification of C-terminal peptides of bovine β-casein that enhance proliferation of rat lymphocytes. Immunology Letters 33 41-46.
    • (1992) Immunology Letters , vol.33 , pp. 41-46
    • Coste, M.1    Rochet, V.2    Lèonil, J.3    Mollè, D.4    Bouhallab, S.5    Tomè, D.6
  • 14
    • 0036252092 scopus 로고    scopus 로고
    • Cationic peptides distribution and mechanism of resistance
    • Devin D A and Hancock R E W (2002) Cationic peptides distribution and mechanism of resistance. Current Pharmaceutical Design 8 703-714.
    • (2002) Current Pharmaceutical Design , vol.8 , pp. 703-714
    • Devin, D.A.1    Hancock, R.E.W.2
  • 15
    • 0031115106 scopus 로고    scopus 로고
    • Antibacterial peptides of bovine lactoferrin: Purification and characterization
    • Dionysius D A and Milne J M (1997) Antibacterial peptides of bovine lactoferrin: purification and characterization. Journal of Dairy Science 80 667-674.
    • (1997) Journal of Dairy Science , vol.80 , pp. 667-674
    • Dionysius, D.A.1    Milne, J.M.2
  • 16
  • 17
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R C and Vogel H J (1999) Diversity of antimicrobial peptides and their mechanisms of action. Biochimica et Biophysica Acta 1462 11-28.
    • (1999) Biochimica et Biophysica Acta , vol.1462 , pp. 11-28
    • Epand, R.C.1    Vogel, H.J.2
  • 18
    • 0014959663 scopus 로고
    • Isolation of bradykinin-potentiating peptides from Bothropsjararaca venom
    • Ferreira S H, Bartet D C and Greene L J (1970) Isolation of bradykinin-potentiating peptides from Bothropsjararaca venom. Biochemistry 9 2583-2593.
    • (1970) Biochemistry , vol.9 , pp. 2583-2593
    • Ferreira, S.H.1    Bartet, D.C.2    Greene, L.J.3
  • 19
    • 0027357826 scopus 로고
    • Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities
    • Fiat A M, Migliore-Samour D, Jollès P, Drouet L, Sollier C B D and Caen J (1993) Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities. Journal of Dairy Science 76 301-310.
    • (1993) Journal of Dairy Science , vol.76 , pp. 301-310
    • Fiat, A.M.1    Migliore-Samour, D.2    Jollès, P.3    Drouet, L.4    Sollier, C.B.D.5    Caen, J.6
  • 20
    • 0032076415 scopus 로고    scopus 로고
    • Potential uses of caseinophosphopeptides
    • FitzGerald R J (1998) Potential uses of caseinophosphopeptides. International Dairy Journal 8 451-457.
    • (1998) International Dairy Journal , vol.8 , pp. 451-457
    • FitzGerald, R.J.1
  • 21
    • 0034492049 scopus 로고    scopus 로고
    • Milk protein derived peptide inhibitors of angiotensin-I-converting enzyme
    • FitzGerald R J and Meisel H (2000) Milk protein derived peptide inhibitors of angiotensin-I-converting enzyme. The British Journal of Nutrition 84 S33-S37.
    • (2000) The British Journal of Nutrition , vol.84
    • FitzGerald, R.J.1    Meisel, H.2
  • 22
    • 0038058813 scopus 로고    scopus 로고
    • Antibacterial and antiviral effects of milk proteins and derivatives thereof
    • Floris R, Recio I, Berkhout B and Visser S (2003) Antibacterial and antiviral effects of milk proteins and derivatives thereof. Current Pharmaceutical Design 9 1257-1273.
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1257-1273
    • Floris, R.1    Recio, I.2    Berkhout, B.3    Visser, S.4
  • 23
    • 0037738603 scopus 로고    scopus 로고
    • Lactic acid bacteria: Inhibition of angiotensin converting enzyme in vitro and in vivo
    • Fuglsang A, Rattray F P, Nilsson D and Nyborg N C B (2003) Lactic acid bacteria: inhibition of angiotensin converting enzyme in vitro and in vivo. Antonie Van Leeuwenhoek 87 27-34.
    • (2003) Antonie Van Leeuwenhoek , vol.87 , pp. 27-34
    • Fuglsang, A.1    Rattray, F.P.2    Nilsson, D.3    Nyborg, N.C.B.4
  • 26
    • 0033823597 scopus 로고    scopus 로고
    • Production of angiotensin-I converting enzyme (ACE)-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4
    • Gobbetti M, Ferranti P, Smacchi E, Goffredi F and Addeo F (2000) Production of angiotensin-I converting enzyme (ACE)-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Applied and Environmental Microbiology 66, 3898-3904.
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 3898-3904
    • Gobbetti, M.1    Ferranti, P.2    Smacchi, E.3    Goffredi, F.4    Addeo, F.5
  • 29
    • 0033174892 scopus 로고    scopus 로고
    • Purification and identification of potentially bioactive peptides from enzyme-modified cheese
    • Haileselassie S, Lee B H and Gibbs B F (1999) Purification and identification of potentially bioactive peptides from enzyme-modified cheese. Journal of Dairy Science 82 1612-1627.
    • (1999) Journal of Dairy Science , vol.82 , pp. 1612-1627
    • Haileselassie, S.1    Lee, B.H.2    Gibbs, B.F.3
  • 30
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock R E W and Leher R (1998) Cationic peptides: a new source of antibiotics. Trends in Biotechnology 16 82-88.
    • (1998) Trends in Biotechnology , vol.16 , pp. 82-88
    • Hancock, R.E.W.1    Leher, R.2
  • 31
    • 0032213421 scopus 로고    scopus 로고
    • s1-casein digest as a factor influencing proliferation and immunoglobulin production in lymphocyte cultures
    • s1-casein digest as a factor influencing proliferation and immunoglobulin production in lymphocyte cultures. Journal of Dairy Research 65 569-578.
    • (1998) Journal of Dairy Research , vol.65 , pp. 569-578
    • Hata, I.1    Higashiyama, S.2    Otani, H.3
  • 32
    • 0040531807 scopus 로고    scopus 로고
    • Immunostimulatory action of a commercially available casein phosphopeptide preparation, CPP-III, in cell culture
    • Hata I, Ueda J and Otani H (1999) Immunostimulatory action of a commercially available casein phosphopeptide preparation, CPP-III, in cell culture. Milchwissenschaft 54 3-7.
    • (1999) Milchwissenschaft , vol.54 , pp. 3-7
    • Hata, I.1    Ueda, J.2    Otani, H.3
  • 34
    • 0016024716 scopus 로고
    • A rennin-sensitive bond in alpha and beta casein
    • Hill R D, Lahov E and Givol D (1974) A rennin-sensitive bond in alpha and beta casein. Journal of Dairy Research 41 147-153.
    • (1974) Journal of Dairy Research , vol.41 , pp. 147-153
    • Hill, R.D.1    Lahov, E.2    Givol, D.3
  • 36
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • Ibrahim H R, Thomas U and Pellegrini A (2001) A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. Journal of Biological Chemistry 276 43767-43774.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 37
  • 41
  • 42
    • 0029924099 scopus 로고    scopus 로고
    • Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins
    • Kayser H and Meisel H (1996) Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Letters 383 18-20.
    • (1996) FEBS Letters , vol.383 , pp. 18-20
    • Kayser, H.1    Meisel, H.2
  • 43
    • 0030041615 scopus 로고    scopus 로고
    • Antibacterial and immunostimulating casein-derived substances from milk: Casecidin, isracidin peptides
    • Lahov E and Regelson W (1996) Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food and Chemical Toxicology 34 131-145.
    • (1996) Food and Chemical Toxicology , vol.34 , pp. 131-145
    • Lahov, E.1    Regelson, W.2
  • 44
    • 0011394385 scopus 로고
    • Properties of basic glycopeptides released from cow milk protein by heat
    • Lahov E, Edelsten D, Sode-Morgensen M T and Sofer E (1971) Properties of basic glycopeptides released from cow milk protein by heat. Milchwissenschaft 26 489-495.
    • (1971) Milchwissenschaft , vol.26 , pp. 489-495
    • Lahov, E.1    Edelsten, D.2    Sode-Morgensen, M.T.3    Sofer, E.4
  • 47
    • 0028438376 scopus 로고
    • A cell culture model to identify biologically active peptides generated by bacterial hydrolysis of casein
    • MacDonald R S, Thornton W H and Marshall R T (1994) A cell culture model to identify biologically active peptides generated by bacterial hydrolysis of casein. Journal of Dairy Science 77 1167-1175.
    • (1994) Journal of Dairy Science , vol.77 , pp. 1167-1175
    • MacDonald, R.S.1    Thornton, W.H.2    Marshall, R.T.3
  • 48
    • 0030202780 scopus 로고    scopus 로고
    • Isolation of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790
    • Maeno M, Yamamoto N and Takano T (1996) Isolation of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790. Journal of Dairy Science 79 1316-1321.
    • (1996) Journal of Dairy Science , vol.79 , pp. 1316-1321
    • Maeno, M.1    Yamamoto, N.2    Takano, T.3
  • 50
    • 2442693700 scopus 로고
    • A peptide inhibitor of angiotensin-I-converting enzyme in the tryptic hydrolysate of casein
    • Maruyama S and Suzuki H (1993) A peptide inhibitor of angiotensin-I-converting enzyme in the tryptic hydrolysate of casein. Agricultural and Biological Chemistry 46 393-1394.
    • (1993) Agricultural and Biological Chemistry , vol.46 , pp. 393-1394
    • Maruyama, S.1    Suzuki, H.2
  • 52
    • 0023218568 scopus 로고
    • Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein
    • Maruyama S, Mitachi H, Tanaka H, Tomizuka N and Suzuki H (1987b) Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein. Agricultural and Biological Chemistry 51 1581-1586.
    • (1987) Agricultural and Biological Chemistry , vol.51 , pp. 1581-1586
    • Maruyama, S.1    Mitachi, H.2    Tanaka, H.3    Tomizuka, N.4    Suzuki, H.5
  • 53
    • 0021888747 scopus 로고
    • Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and the ileum of rats
    • Maruyama S, Nakagomi K, Tomizuka N and Suzuki H (1985) Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. II. Isolation and bradykinin-potentiating activity on the uterus and the ileum of rats. Agricultural and Biological Chemistry 49 1405-1409.
    • (1985) Agricultural and Biological Chemistry , vol.49 , pp. 1405-1409
    • Maruyama, S.1    Nakagomi, K.2    Tomizuka, N.3    Suzuki, H.4
  • 54
    • 0022551001 scopus 로고
    • Chemical characterization and opioid activity of an exorphin isolated from in vivo digests of casein
    • Meisel H (1986) Chemical characterization and opioid activity of an exorphin isolated from in vivo digests of casein. FEBS Letters 196 223-227.
    • (1986) FEBS Letters , vol.196 , pp. 223-227
    • Meisel, H.1
  • 55
    • 0002350154 scopus 로고
    • Casokinins as inhibitors of angiotensin-converting-enzyme
    • Sawatzki G and Renner B, eds. New York: Thieme
    • Meisel H (1993) Casokinins as inhibitors of angiotensin-converting-enzyme. In New Perspectives in Infant Nutrition, pp 153-159. Sawatzki G and Renner B, eds. New York: Thieme.
    • (1993) New Perspectives in Infant Nutrition , pp. 153-159
    • Meisel, H.1
  • 56
    • 0001586967 scopus 로고    scopus 로고
    • Biochemical properties of bioactive peptides derived from milk proteins: Potential nutraceuticals for food and pharmaceutical applications
    • Meisel H (1997) Biochemical properties of bioactive peptides derived from milk proteins: potential nutraceuticals for food and pharmaceutical applications. Livestock Production Science 50 125-138.
    • (1997) Livestock Production Science , vol.50 , pp. 125-138
    • Meisel, H.1
  • 57
    • 0039246617 scopus 로고    scopus 로고
    • Bioactive peptides from milk proteins: A perspective for consumers and producers
    • Meisel H (2001) Bioactive peptides from milk proteins: a perspective for consumers and producers. Australian Journal of Dairy Technology 56 83-91.
    • (2001) Australian Journal of Dairy Technology , vol.56 , pp. 83-91
    • Meisel, H.1
  • 58
    • 0040737822 scopus 로고
    • Isolation and characterization of a phosphopeptide from in vivo digests of casein
    • Barth C A and Schlimme E, eds. Darmstadt: Steinkopf Verlag
    • Meisel H and Frister H (1988) Isolation and characterization of a phosphopeptide from in vivo digests of casein. In Milk Proteins Nutritional, Chemical, Functional and Technological Aspects, pp 150-154. Barth C A and Schlimme E, eds. Darmstadt: Steinkopf Verlag.
    • (1988) Milk Proteins Nutritional, Chemical, Functional and Technological Aspects , pp. 150-154
    • Meisel, H.1    Frister, H.2
  • 59
    • 0038402103 scopus 로고    scopus 로고
    • Food proteins as precursor of peptides modulating human cell activity
    • Meisel H and Günther S (1998) Food proteins as precursor of peptides modulating human cell activity. Nahrung/Food 42 175-176.
    • (1998) Nahrung/Food , vol.42 , pp. 175-176
    • Meisel, H.1    Günther, S.2
  • 60
    • 0032547716 scopus 로고    scopus 로고
    • Estimation of calcium-binding constants of casein phosphopeptides by capillary zone electrophoresis
    • Meisel H and Olieman C (1998) Estimation of calcium-binding constants of casein phosphopeptides by capillary zone electrophoresis. Analytica Chimica Acta 372 291-297.
    • (1998) Analytica Chimica Acta , vol.372 , pp. 291-297
    • Meisel, H.1    Olieman, C.2
  • 62
    • 0002554452 scopus 로고
    • Inhibitors of angiotensin-converting-enzyme derived from bovine casein (casokinins)
    • Brantl V and Teschemacher H, eds. Weinheim: VCH
    • Meisel H and Schlimme E (1994) Inhibitors of angiotensin-converting-enzyme derived from bovine casein (casokinins). In β-Casomorphins and Related Peptides: Recent Developments, pp 27-33. Brantl V and Teschemacher H, eds. Weinheim: VCH.
    • (1994) β-Casomorphins and Related Peptides: Recent Developments , pp. 27-33
    • Meisel, H.1    Schlimme, E.2
  • 65
    • 0032555332 scopus 로고    scopus 로고
    • Apoptosis induced by modified ribonucleosides in human cell culture systems
    • Meisel H, Günther S, Martin D and Schlimme E (1998) Apoptosis induced by modified ribonucleosides in human cell culture systems. FEBS Letters 433 265-268.
    • (1998) FEBS Letters , vol.433 , pp. 265-268
    • Meisel, H.1    Günther, S.2    Martin, D.3    Schlimme, E.4
  • 66
    • 0024329210 scopus 로고
    • Biologically active casein peptides implicated in immunomodulation
    • Migliore-Samour D, Floc'h F and Jollès P (1989) Biologically active casein peptides implicated in immunomodulation. Journal of Dairy Research 56 357-362.
    • (1989) Journal of Dairy Research , vol.56 , pp. 357-362
    • Migliore-Samour, D.1    Floc'h, F.2    Jollès, P.3
  • 67
    • 0141816841 scopus 로고    scopus 로고
    • Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species
    • Minervini F, Algaron F, Rizzello C G, Fox P F, Monnet V and Gobbetti M (2003) Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology 69 5297-5305.
    • (2003) Applied and Environmental Microbiology , vol.69 , pp. 5297-5305
    • Minervini, F.1    Algaron, F.2    Rizzello, C.G.3    Fox, P.F.4    Monnet, V.5    Gobbetti, M.6
  • 68
    • 0029937138 scopus 로고    scopus 로고
    • Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity
    • Mullally M, Meisel H and FitzGerald R J (1996) Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity. Biological Chemistry Hoppe-Seyler 377 259-260.
    • (1996) Biological Chemistry Hoppe-Seyler , vol.377 , pp. 259-260
    • Mullally, M.1    Meisel, H.2    FitzGerald, R.J.3
  • 69
    • 0031055268 scopus 로고    scopus 로고
    • Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic digest of bovine β-lactoglobulin
    • Mullally M, Meisel H and FitzGerald R J (1997) Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic digest of bovine β-lactoglobulin. FEBS Letters 402 99-101.
    • (1997) FEBS Letters , vol.402 , pp. 99-101
    • Mullally, M.1    Meisel, H.2    FitzGerald, R.J.3
  • 73
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin
    • Pellegrini A, Dettling C, Thomas U and Hunziker P (2001) Isolation and characterization of four bactericidal domains in the bovine β -lactoglobulin. Biochimica et Biophysica Acta 1526 131-140.
    • (2001) Biochimica et Biophysica Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 74
    • 0020321280 scopus 로고
    • Angiotensin converting enzyme inhibitors: Medicinal chemistry and biological actions
    • Petrillo E W Jr and Ondetti M A (1982) Angiotensin converting enzyme inhibitors: medicinal chemistry and biological actions. Medicinal Research Reviews 2 1-41.
    • (1982) Medicinal Research Reviews , vol.2 , pp. 1-41
    • Petrillo Jr., E.W.1    Ondetti, M.A.2
  • 75
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: Opioid and ACE-inhibitory peptides
    • Pihlanto-Leppälä A (2001) Bioactive peptides derived from bovine whey proteins: opioid and ACE-inhibitory peptides. Trends in Food Science and Technology 11 347-356.
    • (2001) Trends in Food Science and Technology , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 76
    • 0032047290 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides from bovine milk proteins
    • Pihlanto-Leppälä A, Rokka T and Korhonen H (1998) Angiotensin I converting enzyme inhibitory peptides from bovine milk proteins. International Dairy Journal 8 325-331.
    • (1998) International Dairy Journal , vol.8 , pp. 325-331
    • Pihlanto-Leppälä, A.1    Rokka, T.2    Korhonen, H.3
  • 77
    • 0028833015 scopus 로고
    • Isolation and characterization of sheep lactoferrin, in an inhibitor of platelet aggregation and comparison with human lactoferrin
    • Quian S Y, Jollès P, Migliore-Samour D and Fiat A M (1995) Isolation and characterization of sheep lactoferrin, in an inhibitor of platelet aggregation and comparison with human lactoferrin. Biochimica et Biophysica Acta 1243 25-32.
    • (1995) Biochimica et Biophysica Acta , vol.1243 , pp. 25-32
    • Quian, S.Y.1    Jollès, P.2    Migliore-Samour, D.3    Fiat, A.M.4
  • 78
    • 0032781494 scopus 로고    scopus 로고
    • Identification of two distinct antibacterial domains within the sequence of bovine alpha(s2)-casein
    • Recio I and Visser S (1999) Identification of two distinct antibacterial domains within the sequence of bovine alpha(s2)-casein. Biochimica et Biophysica Acta 1428 314-326.
    • (1999) Biochimica et Biophysica Acta , vol.1428 , pp. 314-326
    • Recio, I.1    Visser, S.2
  • 79
    • 0034488923 scopus 로고    scopus 로고
    • Antibacterial and binding characteristics of bovine, ovine and caprine lactoferrins: A comparative study
    • Recio I and Visser S (2000) Antibacterial and binding characteristics of bovine, ovine and caprine lactoferrins: a comparative study. International Dairy Journal 10 597-605.
    • (2000) International Dairy Journal , vol.10 , pp. 597-605
    • Recio, I.1    Visser, S.2
  • 81
    • 0040511030 scopus 로고    scopus 로고
    • Release of bioactive peptides by enzymatic proteolysis of Lactobacillus GG fermented UHT milk
    • Rokka T, Syvoja E L, Tuominen J and Korhonen H (1997) Release of bioactive peptides by enzymatic proteolysis of Lactobacillus GG fermented UHT milk. Milchwissenschaft 52 675-678.
    • (1997) Milchwissenschaft , vol.52 , pp. 675-678
    • Rokka, T.1    Syvoja, E.L.2    Tuominen, J.3    Korhonen, H.4
  • 84
    • 84984458687 scopus 로고
    • Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects
    • Schlimme E and Meisel H (1995) Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects. Die Nahrung 39 1-20.
    • (1995) Die Nahrung , vol.39 , pp. 1-20
    • Schlimme, E.1    Meisel, H.2
  • 87
    • 0032103233 scopus 로고    scopus 로고
    • Peptides from several Italian cheeses inhibitory to proteolytic enzymes of lactic acid bacteria, Pseudomonas fluorescens ATCC 948 and to the angiotensin I-converting enzyme
    • Smacchi E and Gobbetti M (1998) Peptides from several Italian cheeses inhibitory to proteolytic enzymes of lactic acid bacteria, Pseudomonas fluorescens ATCC 948 and to the angiotensin I-converting enzyme. Enzyme and Microbial Technology 22 687-694.
    • (1998) Enzyme and Microbial Technology , vol.22 , pp. 687-694
    • Smacchi, E.1    Gobbetti, M.2
  • 88
    • 0000420163 scopus 로고
    • Effect of peptides from the sequence 58-72 of β-casein on the activity of endopeptidase, aminopeptidase and X-prolyldipeptidyl aminopeptidase from Lactococcus
    • Stepaniak L, Fox P F, Sørhaug T and Grabska J J (1995) Effect of peptides from the sequence 58-72 of β-casein on the activity of endopeptidase, aminopeptidase and X-prolyldipeptidyl aminopeptidase from Lactococcus. Journal of Agricultural and Food Chemistry 45 849-853.
    • (1995) Journal of Agricultural and Food Chemistry , vol.45 , pp. 849-853
    • Stepaniak, L.1    Fox, P.F.2    Sørhaug, T.3    Grabska, J.J.4
  • 91
    • 0034492053 scopus 로고    scopus 로고
    • Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics
    • Vegarud G E, Langsrud T and Svenning C (2000) Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics. British Journal of Nutrition 58 91-98.
    • (2000) British Journal of Nutrition , vol.58 , pp. 91-98
    • Vegarud, G.E.1    Langsrud, T.2    Svenning, C.3
  • 93
    • 0035188986 scopus 로고    scopus 로고
    • An in vivo study of novel bioactive peptides that inhibit the growth of Escherichia coli
    • Walker J R, Roth J R and Altman E (2001) An in vivo study of novel bioactive peptides that inhibit the growth of Escherichia coli. Journal of Peptide Research 58 380-388.
    • (2001) Journal of Peptide Research , vol.58 , pp. 380-388
    • Walker, J.R.1    Roth, J.R.2    Altman, E.3
  • 94
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht T, Dathe M, Epand R M, Beyermann M, Krause E, Maloy W L, MacDonald D L and Bienert M (1997) Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry 36 12869-12880.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 95
    • 0030873439 scopus 로고    scopus 로고
    • Antihypertensive peptides derived from food proteins
    • Yamamoto N (1997) Antihypertensive peptides derived from food proteins. Biopolymers 43 129-134.
    • (1997) Biopolymers , vol.43 , pp. 129-134
    • Yamamoto, N.1
  • 96
    • 85008124093 scopus 로고
    • Antihypertensive effect of different kinds of fermented milk in spontaneously hypertensive rats
    • Yamamoto N, Akino A and Takano T (1994a) Antihypertensive effect of different kinds of fermented milk in spontaneously hypertensive rats. Bioscience, Biotechnology, and Biochemistry 58 776-778.
    • (1994) Bioscience, Biotechnology, and Biochemistry , vol.58 , pp. 776-778
    • Yamamoto, N.1    Akino, A.2    Takano, T.3
  • 97
    • 0028414339 scopus 로고
    • Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790
    • Yamamoto N, Akino A and Takano T (1994b) Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790. Journal of Dairy Science 77 917-922.
    • (1994) Journal of Dairy Science , vol.77 , pp. 917-922
    • Yamamoto, N.1    Akino, A.2    Takano, T.3
  • 98
    • 0033161658 scopus 로고    scopus 로고
    • Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by Lactobacillus helveticus CPN4
    • Yamamoto N, Maeno M and Takano T (1999) Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by Lactobacillus helveticus CPN4. Journal of Dairy Science 82 1388-1393.
    • (1999) Journal of Dairy Science , vol.82 , pp. 1388-1393
    • Yamamoto, N.1    Maeno, M.2    Takano, T.3
  • 99
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi K, Tomita M, Giehl T J and Ellison R T III (1993) Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infection and Immunity 61 719-728.
    • (1993) Infection and Immunity , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison III, R.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.