메뉴 건너뛰기




Volumn 76, Issue 7, 2011, Pages

Egg Yolk Phosvitin and Functional Phosphopeptides-Review

Author keywords

Antioxidant; Lipid oxidation; Mineral binding; Phosphopeptides; Phosvitin

Indexed keywords

AMINO ACID; ANTIINFECTIVE AGENT; ANTIOXIDANT; CHELATING AGENT; EMULSIFYING AGENT; MINERAL; PHOSPHOPEPTIDE; PHOSVITIN;

EID: 80053050275     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2011.02291.x     Document Type: Review
Times cited : (97)

References (118)
  • 1
    • 0037841336 scopus 로고
    • Fractionation and characterization of hen's egg yolk phosvitin
    • Abe Y, Itoh T, Adachi S. 1982. Fractionation and characterization of hen's egg yolk phosvitin. J Food Sci 47(6):1903-7.
    • (1982) J Food Sci , vol.47 , Issue.6 , pp. 1903-1907
    • Abe, Y.1    Itoh, T.2    Adachi, S.3
  • 2
    • 17744407094 scopus 로고    scopus 로고
    • Iron tissue storage and hemoglobin levels of deficient repleted with iron bound to the caseinophosphopeptide 1-25 of beta-casein
    • Aït-Oukhatar N, Bouhallab S, Arhan P, Maubois JL, Drosdowsky M, Bouglé D. 1999. Iron tissue storage and hemoglobin levels of deficient repleted with iron bound to the caseinophosphopeptide 1-25 of beta-casein. J Agric Food Chem 47:2786-90.
    • (1999) J Agric Food Chem , vol.47 , pp. 2786-2790
    • Aït-Oukhatar, N.1    Bouhallab, S.2    Arhan, P.3    Maubois, J.L.4    Drosdowsky, M.5    Bouglé, D.6
  • 3
    • 84985216722 scopus 로고
    • Release of iron from phosvitin by heat and food additives
    • Albright KJ, Gordon DT, Cotterill OJ. 1984. Release of iron from phosvitin by heat and food additives. J Food Sci 49:78-81.
    • (1984) J Food Sci , vol.49 , pp. 78-81
    • Albright, K.J.1    Gordon, D.T.2    Cotterill, O.J.3
  • 4
    • 80053052601 scopus 로고    scopus 로고
    • Isolation and characterization of CPP (casein phosphopeptides) from fermented milk
    • Arunachalam KD, Raja RB. 2010. Isolation and characterization of CPP (casein phosphopeptides) from fermented milk. Afr J Food Sci 4:167-75.
    • (2010) Afr J Food Sci , vol.4 , pp. 167-175
    • Arunachalam, K.D.1    Raja, R.B.2
  • 6
    • 0004126991 scopus 로고
    • Preserving food and health: antioxidants make functional, nutritious preservatives
    • Becker GL. 1993. Preserving food and health: antioxidants make functional, nutritious preservatives. Food Pro 12:54-6.
    • (1993) Food Pro , vol.12 , pp. 54-56
    • Becker, G.L.1
  • 7
    • 0003895440 scopus 로고    scopus 로고
    • forth revised and extended edition. Berlin, Heidelberg Springer-Verlag.
    • Belitz HB, Grosch W, Schieberle P. 2009. Food Chemistry, forth revised and extended edition. Berlin, Heidelberg Springer-Verlag. 1070 p.
    • (2009) Food Chemistry , pp. 1070
    • Belitz, H.B.1    Grosch, W.2    Schieberle, P.3
  • 9
    • 0016469166 scopus 로고
    • Toxicology and biochemistry of butylated hydroxyanisole and butylated hydroxytoluene
    • Branen AL. 1975. Toxicology and biochemistry of butylated hydroxyanisole and butylated hydroxytoluene. J Am Oil Chem Soc 52:59-63.
    • (1975) J Am Oil Chem Soc , vol.52 , pp. 59-63
    • Branen, A.L.1
  • 10
    • 0025340673 scopus 로고
    • Structure of the oligosaccharide of hen phosvitin as determined by two-dimensional 1H NMR of the intact glycoprotein
    • Brockbank RL, Vogel HJ. 1990. Structure of the oligosaccharide of hen phosvitin as determined by two-dimensional 1H NMR of the intact glycoprotein. Biochem 12:5574-83.
    • (1990) Biochem , vol.12 , pp. 5574-5583
    • Brockbank, R.L.1    Vogel, H.J.2
  • 11
    • 0000154785 scopus 로고
    • Isolation and composition of avian egg yolk granules and their constituents α- and β-lipovitellins
    • Burley RW, Cook WH. 1961. Isolation and composition of avian egg yolk granules and their constituents α- and β-lipovitellins. Can J Biochem 39:1295-307.
    • (1961) Can J Biochem , vol.39 , pp. 1295-1307
    • Burley, R.W.1    Cook, W.H.2
  • 12
    • 0021760617 scopus 로고
    • Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene
    • Byrne BM, van Het Schip AD, van de Klundert JAM, Arnberg AC, Gruber M, Geert AB. 1984. Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene. Biochem 23:4275-9.
    • (1984) Biochem , vol.23 , pp. 4275-4279
    • Byrne, B.M.1    van Het Schip, A.D.2    van de Klundert, J.A.M.3    Arnberg, A.C.4    Gruber, M.5    Geert, A.B.6
  • 15
    • 0942300631 scopus 로고    scopus 로고
    • Influence of physicochemical conditions and technological treatments on the iron binding capacity of egg yolk phosvitin
    • Castellani O, Guérin-Dubiard C, David-Briand E, Anton M. 2004. Influence of physicochemical conditions and technological treatments on the iron binding capacity of egg yolk phosvitin. Food Chem 85:569-77.
    • (2004) Food Chem , vol.85 , pp. 569-577
    • Castellani, O.1    Guérin-Dubiard, C.2    David-Briand, E.3    Anton, M.4
  • 16
    • 0001302366 scopus 로고
    • EPR spin-trapping studies of the hydroxyl radical scavenging activity of carnosine and related dipeptides
    • Chan WKM, Decker EA, Lee JB, Butterfield DA. 1994. EPR spin-trapping studies of the hydroxyl radical scavenging activity of carnosine and related dipeptides. J Agr Food Chem 42 (7):1407-10.
    • (1994) J Agr Food Chem , vol.42 , Issue.7 , pp. 1407-1410
    • Chan, W.K.M.1    Decker, E.A.2    Lee, J.B.3    Butterfield, D.A.4
  • 17
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the β-turns
    • Chang CT, Wu CSC, Yang JT. 1978. Circular dichroic analysis of protein conformation: Inclusion of the β-turns. Anal Biochem 91:13-31.
    • (1978) Anal Biochem , Issue.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.S.C.2    Yang, J.T.3
  • 18
    • 11144228135 scopus 로고    scopus 로고
    • Antioxidant characterization of caseinphosphopeptides from bovine milk
    • In: Shahidi F, Weerasinghe DK, editors. Washington, D.C. Oxford Press. p -
    • Chiu SCK, Kitts DD. 2004. Antioxidant characterization of caseinphosphopeptides from bovine milk. In: Shahidi F, Weerasinghe DK, editors. Nutraceutical beverages: Chemistry, nutrition and health effects. Washington, D.C. Oxford Press. p 279-89.
    • (2004) Nutraceutical beverages: Chemistry, nutrition and health effects , pp. 279-289
    • Chiu, S.C.K.1    Kitts, D.D.2
  • 19
    • 20444424986 scopus 로고    scopus 로고
    • Effectiveness of phosvitin peptides on enhancing bioavailability of calcium and its accumulation in bones
    • Choi I, Jung C, Choi H, Kim C, Ha H. 2005. Effectiveness of phosvitin peptides on enhancing bioavailability of calcium and its accumulation in bones. Food Chem 93:577-83.
    • (2005) Food Chem , vol.93 , pp. 577-583
    • Choi, I.1    Jung, C.2    Choi, H.3    Kim, C.4    Ha, H.5
  • 20
    • 0000010770 scopus 로고
    • Interrelationships of cellular antioxidant defense systems
    • In: How CK, editor., Vol Boca Raton, Fla. CRC Press, p -
    • Chow CK. 1988. Interrelationships of cellular antioxidant defense systems. In: How CK, editor. Cellular antioxidant defense mechanisms, Vol II. Boca Raton, Fla. CRC Press, p 217-37.
    • (1988) Cellular antioxidant defense mechanisms , vol.2 , pp. 217-237
    • Chow, C.K.1
  • 21
    • 0002611152 scopus 로고
    • pH and sodium chloride effects on emulsifying properties of egg yolk phosvitin
    • Chung SL, Ferrier KL. 1992. pH and sodium chloride effects on emulsifying properties of egg yolk phosvitin. J Food Sci 57(1):40-2.
    • (1992) J Food Sci , vol.57 , Issue.1 , pp. 40-42
    • Chung, S.L.1    Ferrier, K.L.2
  • 22
    • 0008552289 scopus 로고
    • Heat denaturation and emulsifying properties of egg yolk phosvitin
    • Chung SL, Ferrier LK. 1995. Heat denaturation and emulsifying properties of egg yolk phosvitin. J Food Sci 60(5):906-8.
    • (1995) J Food Sci , vol.60 , Issue.5 , pp. 906-908
    • Chung, S.L.1    Ferrier, L.K.2
  • 23
    • 84985201066 scopus 로고
    • Conditions affecting emulsifying properties of egg yolk phosvitin
    • Chung SL, Ferrier LK. 1991. Conditions affecting emulsifying properties of egg yolk phosvitin. J Food Sci 56(5):1259-62.
    • (1991) J Food Sci , vol.56 , Issue.5 , pp. 1259-1262
    • Chung, S.L.1    Ferrier, L.K.2
  • 24
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: a prospectus
    • Clare DA, Swaisgood HE. 2000. Bioactive milk peptides: a prospectus. J Dairy Sci 83:1187-95.
    • (2000) J Dairy Sci , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 25
    • 49649149408 scopus 로고
    • A comparison of the heterogeneity of phosvitin of egg-yolk and blood-plasma of the domestic fowl (Gallus domesticus)
    • Culbert J, McIndoe WM. 1971. A comparison of the heterogeneity of phosvitin of egg-yolk and blood-plasma of the domestic fowl (Gallus domesticus) Int J Biochem 2 (12):617-22.
    • (1971) Int J Biochem , vol.2 , Issue.12 , pp. 617-622
    • Culbert, J.1    McIndoe, W.M.2
  • 27
    • 11144231660 scopus 로고    scopus 로고
    • Antioxidant mechanisms of caseinophosphopeptides and casein hydrolysates and their application in ground beef
    • Díaz M, Decker EA. 2004. Antioxidant mechanisms of caseinophosphopeptides and casein hydrolysates and their application in ground beef. J Agric Food Chem 52:8208-13.
    • (2004) J Agric Food Chem , vol.52 , pp. 8208-8213
    • Díaz, M.1    Decker, E.A.2
  • 28
    • 0037427217 scopus 로고    scopus 로고
    • Use of caseinophosphopeptides as natural antioxidant in oil-in-water emulsions
    • Díaz M, Dunn CM, McClements DJ, Decker EA. 2003. Use of caseinophosphopeptides as natural antioxidant in oil-in-water emulsions. J Agric Food Chem 51:2365-70.
    • (2003) J Agric Food Chem , vol.51 , pp. 2365-2370
    • Díaz, M.1    Dunn, C.M.2    McClements, D.J.3    Decker, E.A.4
  • 30
    • 0017106742 scopus 로고
    • Involvement of polyphosphorylserine blocks in the Fe(III) binding by phosvitin
    • Donella A, Pinna LA, Moret V. 1976. Involvement of polyphosphorylserine blocks in the Fe(III) binding by phosvitin. Chem Biol Interact 15(2):165-71.
    • (1976) Chem Biol Interact , vol.15 , Issue.2 , pp. 165-171
    • Donella, A.1    Pinna, L.A.2    Moret, V.3
  • 32
    • 0026568707 scopus 로고
    • Iron oxidation by casein
    • Emery T. 1992. Iron oxidation by casein. Biochem Bioph Res Co 182:1047-52.
    • (1992) Biochem Bioph Res Co , vol.182 , pp. 1047-1052
    • Emery, T.1
  • 33
    • 0034983668 scopus 로고    scopus 로고
    • Casein phosphopeptides influence calcium uptake by cultured human intestinal HT-29 tumor cells
    • Ferraretto A, Signorile A, Gravaghi C, Fiorilli A, Tettamanti G. 2001. Casein phosphopeptides influence calcium uptake by cultured human intestinal HT-29 tumor cells. J Nutr 131:1655-61.
    • (2001) J Nutr , vol.131 , pp. 1655-1661
    • Ferraretto, A.1    Signorile, A.2    Gravaghi, C.3    Fiorilli, A.4    Tettamanti, G.5
  • 34
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T, Holbrook NJ. 2000. Oxidants, oxidative stress and the biology of ageing. Nature 408:239-47.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 35
    • 0032076415 scopus 로고    scopus 로고
    • Potential uses of caseinophosphopetides
    • FitzGerals RJ. 1998. Potential uses of caseinophosphopetides. Int Dairy J 8:451-7.
    • (1998) Int Dairy J , vol.8 , pp. 451-457
    • FitzGerals, R.J.1
  • 36
    • 0034956439 scopus 로고    scopus 로고
    • Iron fortification in dairy industry
    • Gaucheron F. 2000. Iron fortification in dairy industry. Trends Food Sci Tech 11:403-9.
    • (2000) Trends Food Sci Tech , vol.11 , pp. 403-409
    • Gaucheron, F.1
  • 37
    • 84874499889 scopus 로고    scopus 로고
    • Biologically active peptides and enzymatic approaches to their production
    • Gill R, López-Fandiño XJ, Vulfson EV. 1996. Biologically active peptides and enzymatic approaches to their production. Enzyme Microb Tech 18:162-83.
    • (1996) Enzyme Microb Tech , vol.18 , pp. 162-183
    • Gill, R.1    López-Fandiño, X.J.2    Vulfson, E.V.3
  • 38
    • 0030040892 scopus 로고    scopus 로고
    • Oligophosphopeptides of varied structural complexity derived from the egg phosphoprotein, phosvitin
    • Goulas A, Triplett EL, Taborsky G. 1996. Oligophosphopeptides of varied structural complexity derived from the egg phosphoprotein, phosvitin. J Protein Chem 15:1-9.
    • (1996) J Protein Chem , vol.15 , pp. 1-9
    • Goulas, A.1    Triplett, E.L.2    Taborsky, G.3
  • 40
    • 0014962156 scopus 로고
    • Conformation of the phosphoprotein, phosvitin
    • Grizzuti K, Perlmann GE. 1970. Conformation of the phosphoprotein, phosvitin. J Biol Chem 245:2573-78.
    • (1970) J Biol Chem , vol.245 , pp. 2573-2578
    • Grizzuti, K.1    Perlmann, G.E.2
  • 41
    • 0015899492 scopus 로고
    • Binding of magnesium and calcium ions to the phosphoglycoprotein phosvitin
    • Grizzuti K, Perlmann GE. 1973. Binding of magnesium and calcium ions to the phosphoglycoprotein phosvitin. Biochem 12:4399-403.
    • (1973) Biochem , vol.12 , pp. 4399-4403
    • Grizzuti, K.1    Perlmann, G.E.2
  • 42
    • 0011080880 scopus 로고
    • Studies on the deposition and nature of egg yolk iron
    • Halkett JAE, Peters T, Ross JF. 1958. Studies on the deposition and nature of egg yolk iron. J Biol Chem 231:187-199.
    • (1958) J Biol Chem , vol.231 , pp. 187-199
    • Halkett, J.A.E.1    Peters, T.2    Ross, J.F.3
  • 43
    • 0030730448 scopus 로고    scopus 로고
    • Effect of casein phosphopeptides on zinc and calcium absorption from bread meals
    • Hansen M, Sandström B, Jensen M, Sorensen SS. 1997. Effect of casein phosphopeptides on zinc and calcium absorption from bread meals. J Trace Elem Med Biol 11:143-9.
    • (1997) J Trace Elem Med Biol , vol.11 , pp. 143-149
    • Hansen, M.1    Sandström, B.2    Jensen, M.3    Sorensen, S.S.4
  • 44
    • 0029769496 scopus 로고    scopus 로고
    • The effect of casein phosphopeptides on zinc and calcium absorption from high phytate infant diets assessed in rat pups and Caco-2 cells
    • Hansen M, Sandström B, Lönnerdal B. 1996. The effect of casein phosphopeptides on zinc and calcium absorption from high phytate infant diets assessed in rat pups and Caco-2 cells. Pediatr Res 40:547-52.
    • (1996) Pediatr Res , vol.40 , pp. 547-552
    • Hansen, M.1    Sandström, B.2    Lönnerdal, B.3
  • 45
    • 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
  • 46
    • 0018781475 scopus 로고
    • Iron(III)-phosphoprotein chelates: stoichiometric equilibrium constant for interaction of iron(III) and phosphorylserine residues of phosvitin and casein
    • Hegenauer J, Saltman P, Nace G. 1979. Iron(III)-phosphoprotein chelates: stoichiometric equilibrium constant for interaction of iron(III) and phosphorylserine residues of phosvitin and casein. Biochem 18:3865-79.
    • (1979) Biochem , vol.18 , pp. 3865-3879
    • Hegenauer, J.1    Saltman, P.2    Nace, G.3
  • 47
    • 4544300929 scopus 로고    scopus 로고
    • Egg yolk phosvitin inhibits hydroxyl radical formation from the Fenton reaction
    • Ishikawa S, Yano Y, Arihara K, Itoh M. 2004. Egg yolk phosvitin inhibits hydroxyl radical formation from the Fenton reaction. Biosci Biotech Biochem 68:1324-31.
    • (2004) Biosci Biotech Biochem , vol.68 , pp. 1324-1331
    • Ishikawa, S.1    Yano, Y.2    Arihara, K.3    Itoh, M.4
  • 48
    • 34547829763 scopus 로고    scopus 로고
    • Egg yolk protein and egg yolk phosvitin inhibit calcium, magnesium, and iron absorptions in rats
    • Ishikawa SI, Tamaki S, Arihara K, Itoh M. 2007. Egg yolk protein and egg yolk phosvitin inhibit calcium, magnesium, and iron absorptions in rats. J Food Sci 72:412-9.
    • (2007) J Food Sci , vol.72 , pp. 412-419
    • Ishikawa, S.I.1    Tamaki, S.2    Arihara, K.3    Itoh, M.4
  • 49
    • 0001270728 scopus 로고
    • Comparative studies on the α- and β-phosvitins from hen's egg yolk
    • Itoh T, Abe Y, Adachi S. 1983. Comparative studies on the α- and β-phosvitins from hen's egg yolk. J Food Sci 48:1755-7.
    • (1983) J Food Sci , vol.48 , pp. 1755-1757
    • Itoh, T.1    Abe, Y.2    Adachi, S.3
  • 50
    • 0034055342 scopus 로고    scopus 로고
    • Preparation of novel functional oligophosphopeptides from hen egg yolk phosvitin
    • Jiang B, Mine Y. 2000. Preparation of novel functional oligophosphopeptides from hen egg yolk phosvitin. J Agric Food Chem 48:990-4.
    • (2000) J Agric Food Chem , vol.48 , pp. 990-994
    • Jiang, B.1    Mine, Y.2
  • 51
    • 0035348366 scopus 로고    scopus 로고
    • Phosphopeptides derived from hen egg yolk phosvitin: effect of molecular size on the calcium-binding properties
    • Jiang B, Mine Y. 2001. Phosphopeptides derived from hen egg yolk phosvitin: effect of molecular size on the calcium-binding properties. Biosci Biotech Biochem 65:1187-90.
    • (2001) Biosci Biotech Biochem , vol.65 , pp. 1187-1190
    • Jiang, B.1    Mine, Y.2
  • 52
    • 4944224574 scopus 로고    scopus 로고
    • beta-Caseinophosphopeptide (f1-25) confers on beta-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes
    • Kansci G, Genot C, Meynier A, Gauheron F, Chobert JM. 2004. beta-Caseinophosphopeptide (f1-25) confers on beta-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes. LAIT 84:449-62.
    • (2004) LAIT , vol.84 , pp. 449-462
    • Kansci, G.1    Genot, C.2    Meynier, A.3    Gauheron, F.4    Chobert, J.M.5
  • 53
    • 33244465570 scopus 로고    scopus 로고
    • Antioxidative stress activity of oligophosphopeptides derived from hen egg yolk phosvitin in Caco-2 Cells
    • Katayama S, Xu X, Fan MZ, Mine Y. 2006. Antioxidative stress activity of oligophosphopeptides derived from hen egg yolk phosvitin in Caco-2 Cells. J Agric Food Chem 54:773-8.
    • (2006) J Agric Food Chem , vol.54 , pp. 773-778
    • Katayama, S.1    Xu, X.2    Fan, M.Z.3    Mine, Y.4
  • 54
    • 84987283038 scopus 로고
    • Effects of phosphate residues on the excellent emulsifying properties of phosphoglycoprotein phosvitin
    • Kato A, Miyazaki S, Kawamoto A, Kobayashi K. 1987. Effects of phosphate residues on the excellent emulsifying properties of phosphoglycoprotein phosvitin. Agric Biol Chem 51:2989-94.
    • (1987) Agric Biol Chem , vol.51 , pp. 2989-2994
    • Kato, A.1    Miyazaki, S.2    Kawamoto, A.3    Kobayashi, K.4
  • 55
    • 0032782512 scopus 로고    scopus 로고
    • Molecular mechanism of the excellent emulsifying properties of phosvitin-galactomannan onjugate
    • Khan MSA, Babiker EE, Azakami H, Kato A. 1999. Molecular mechanism of the excellent emulsifying properties of phosvitin-galactomannan onjugate. J Agric Food Chem 47:2262-26.
    • (1999) J Agric Food Chem , vol.47 , pp. 2262-2226
    • Khan, M.S.A.1    Babiker, E.E.2    Azakami, H.3    Kato, A.4
  • 56
    • 0343680582 scopus 로고    scopus 로고
    • Effect of protease digestion and dephosphorylation on high emulsifying properties of hen egg yolk phosvitin
    • Khan SMA, Babiker EE, Azakami H, Kato A. 1998. Effect of protease digestion and dephosphorylation on high emulsifying properties of hen egg yolk phosvitin. J Agric Food Chem 46:4977-81.
    • (1998) J Agric Food Chem , vol.46 , pp. 4977-4981
    • Khan, S.M.A.1    Babiker, E.E.2    Azakami, H.3    Kato, A.4
  • 57
    • 0342803211 scopus 로고    scopus 로고
    • Bactericidal action of egg yolk phosvitin againstEscherichia coliunder thermal Stress
    • Khan SMA, Nakamura S, Ogawa M, Akita E, Azakami H, Kato A. 2000. Bactericidal action of egg yolk phosvitin againstEscherichia coliunder thermal Stress. J Agric Food Chem 48:1503-6.
    • (2000) J Agric Food Chem , vol.48 , pp. 1503-1506
    • Khan, S.M.A.1    Nakamura, S.2    Ogawa, M.3    Akita, E.4    Azakami, H.5    Kato, A.6
  • 58
    • 34249006295 scopus 로고    scopus 로고
    • Antioxidant capacity of caseinophosphopeptides prepared from sodium caseinate using alcalase
    • Kim GN, Jang H, Kim C. 2007. Antioxidant capacity of caseinophosphopeptides prepared from sodium caseinate using alcalase. Food Chem 104:1359-65.
    • (2007) Food Chem , vol.104 , pp. 1359-1365
    • Kim, G.N.1    Jang, H.2    Kim, C.3
  • 59
    • 0028856041 scopus 로고
    • Iron absorption and intestinal solubility in rats are influenced by dietary proteins
    • Kim M, Lee DT, Lee YS. 1995. Iron absorption and intestinal solubility in rats are influenced by dietary proteins. Nutr Res 15:1705-16.
    • (1995) Nutr Res , vol.15 , pp. 1705-1716
    • Kim, M.1    Lee, D.T.2    Lee, Y.S.3
  • 60
    • 0028277567 scopus 로고
    • Bioactive peptides in food: identification and potential uses
    • Kitts DD. 1994. Bioactive peptides in food: identification and potential uses. Can J Physiol Pharm 72:423-34.
    • (1994) Can J Physiol Pharm , vol.72 , pp. 423-434
    • Kitts, D.D.1
  • 61
    • 27944480872 scopus 로고    scopus 로고
    • Antioxidant properties of casein-phosphopeptides
    • Kitts DD. 2005. Antioxidant properties of casein-phosphopeptides. Trends Food Sci Tech 16:549-54.
    • (2005) Trends Food Sci Tech , vol.16 , pp. 549-554
    • Kitts, D.D.1
  • 62
    • 80053051023 scopus 로고    scopus 로고
    • Editors. Lactic acid bacteria: genetics, metabolism, and applications: proceedings of the Sixth Symposium on Lactic Acid Bacteria: Genetics, Metabolism and Applications, Federation of European Microbiological Societies, 1999.
    • Konings WN, Kuipers OP, Huis in't Veld. Editors.September 1999 Lactic acid bacteria: genetics, metabolism, and applications: proceedings of the Sixth Symposium on Lactic Acid Bacteria: Genetics, Metabolism and Applications, 19-23, Veldhoven, The Netherlands, Vol 74-76, Federation of European Microbiological Societies, 1999.
    • (1999) , pp. 19-23
    • Konings, W.N.1    Kuipers, O.P.2    Huis in't, V.3
  • 63
    • 0022568806 scopus 로고
    • Iron mobilization from lactoferrin by cheaters at physiological pH
    • Kontoghiorghes G. 1986. Iron mobilization from lactoferrin by cheaters at physiological pH. Biochim Biophys Acta 882:267-70.
    • (1986) Biochim Biophys Acta , vol.882 , pp. 267-270
    • Kontoghiorghes, G.1
  • 64
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: Production and functionality
    • Korhonen H, Pihlanto A. 2006. Bioactive peptides: Production and functionality. Int Dairy J 16:945-60.
    • (2006) Int Dairy J , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 65
    • 0030041615 scopus 로고    scopus 로고
    • Antibacterial and immunostimulating casein-derived substances from milk: casesidin, isracidin peptides
    • Lahov E, Regelson W. 1996. Antibacterial and immunostimulating casein-derived substances from milk: casesidin, isracidin peptides. Food Chem Toxicol 34:131-45.
    • (1996) Food Chem Toxicol , vol.34 , pp. 131-145
    • Lahov, E.1    Regelson, W.2
  • 66
    • 0036188865 scopus 로고    scopus 로고
    • Antioxidant activity of phosvitin in phosphatidylcholine liposomes and meat model systems
    • Lee SK, Han JH, Decker EA. 2002. Antioxidant activity of phosvitin in phosphatidylcholine liposomes and meat model systems. Food Chem Toxicol 67:37-41.
    • (2002) Food Chem Toxicol , vol.67 , pp. 37-41
    • Lee, S.K.1    Han, J.H.2    Decker, E.A.3
  • 67
    • 0024415827 scopus 로고
    • Indirect effect of casein phosphopeptides on calcium absorption in rat ileum in vitro
    • Li Y, Tomé D, Desjeux JF. 1989. Indirect effect of casein phosphopeptides on calcium absorption in rat ileum in vitro. Reprod Nutr Dev 29:227-33.
    • (1989) Reprod Nutr Dev , vol.29 , pp. 227-233
    • Li, Y.1    Tomé, D.2    Desjeux, J.F.3
  • 68
    • 0022818205 scopus 로고
    • Characteristics of egg yolk phosvitin as an antioxidant for inhibiting metal-catalyzed phospholipid oxidations
    • Lu CL, Baker RC. 1986. Characteristics of egg yolk phosvitin as an antioxidant for inhibiting metal-catalyzed phospholipid oxidations. Poult Sci 65:2065-70.
    • (1986) Poult Sci , vol.65 , pp. 2065-2070
    • Lu, C.L.1    Baker, R.C.2
  • 69
    • 0000645419 scopus 로고
    • Effect of pH and food ingredients on the stability of egg yolk phospholipids and the metal-chelator antioxidant activity of phosvitin
    • Lu CL, Baker RC. 1987. Effect of pH and food ingredients on the stability of egg yolk phospholipids and the metal-chelator antioxidant activity of phosvitin. J Food Sci 52:613-6.
    • (1987) J Food Sci , vol.52 , pp. 613-616
    • Lu, C.L.1    Baker, R.C.2
  • 70
    • 0014075273 scopus 로고
    • The macromolecular composition of hen's egg yolk at successive stages of maturation
    • MacKenzie SI, Martin WG. 1967. The macromolecular composition of hen's egg yolk at successive stages of maturation. Can J Biochem 45:591-601.
    • (1967) Can J Biochem , vol.45 , pp. 591-601
    • MacKenzie, S.I.1    Martin, W.G.2
  • 71
    • 84985292822 scopus 로고
    • Ion-exchange chromatography and electrophoresis of egg yolk proteins
    • McBee LE, Cotterill OJ. 1979. Ion-exchange chromatography and electrophoresis of egg yolk proteins. J Food Sci 44:656-60.
    • (1979) J Food Sci , vol.44 , pp. 656-660
    • McBee, L.E.1    Cotterill, O.J.2
  • 73
    • 0034492226 scopus 로고    scopus 로고
    • Lipid oxidation in oil-in-water emulsions: impact of molecular environment on chemical reactions in heterogeneous food systems
    • McClements DJ, Decker EA. 2000. Lipid oxidation in oil-in-water emulsions: impact of molecular environment on chemical reactions in heterogeneous food systems. J Food Sci 65:1270-82.
    • (2000) J Food Sci , vol.65 , pp. 1270-1282
    • McClements, D.J.1    Decker, E.A.2
  • 74
    • 0008615931 scopus 로고
    • Phosvitin, the principal phosphoprotein of egg yolk
    • Mecham DK, Olcott HS. 1949. Phosvitin, the principal phosphoprotein of egg yolk. J Am Chem Soc 71:3670-9.
    • (1949) J Am Chem Soc , vol.71 , pp. 3670-3679
    • Mecham, D.K.1    Olcott, H.S.2
  • 75
    • 0038397187 scopus 로고    scopus 로고
    • Biofunctional peptides from milk proteins: Mineral binding and cytomodulatory effects
    • Meisel H, Fitzgerald RJ. 2003. Biofunctional peptides from milk proteins: Mineral binding and cytomodulatory effects. Curr Pharm Design 9:1289-95.
    • (2003) Curr Pharm Design , vol.9 , pp. 1289-1295
    • Meisel, H.1    Fitzgerald, R.J.2
  • 76
    • 0001586967 scopus 로고    scopus 로고
    • Biochemical properties of bioactive peptides derived from milk proteins; Potential nutrceuticals for food and pharmaceutical applications
    • Meisel H. 1997a. Biochemical properties of bioactive peptides derived from milk proteins; Potential nutrceuticals for food and pharmaceutical applications. Livest Prod Sci 50:125-38.
    • (1997) Livest Prod Sci , vol.50 , pp. 125-138
    • Meisel, H.1
  • 77
    • 0030749136 scopus 로고    scopus 로고
    • Biochemical properties of regulatory peptides derived from milk proteins
    • Meisel H. 1997b. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 43:119-28.
    • (1997) Biopolymers , vol.43 , pp. 119-128
    • Meisel, H.1
  • 78
    • 0002605217 scopus 로고
    • On chemical and nutritional differences between casein from human and from cow's milk. Upsala
    • Mellander O. 1947. On chemical and nutritional differences between casein from human and from cow's milk. Upsala Läkareforen Förhandl 52:107-8.
    • (1947) Läkareforen Förhandl , vol.52 , pp. 107-108
    • Mellander, O.1
  • 79
    • 13244279441 scopus 로고    scopus 로고
    • Antioxidant properties of a radical scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate
    • Mendis E, Rajapakse N, Kim SK. 2005. Antioxidant properties of a radical scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. J Agric Food Chem 53:581-7.
    • (2005) J Agric Food Chem , vol.53 , pp. 581-587
    • Mendis, E.1    Rajapakse, N.2    Kim, S.K.3
  • 80
    • 0141816841 scopus 로고    scopus 로고
    • Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides fromlactobacillus helveticusPR4 proteinase-hydrolyzed caseins of milk from six species
    • Minervini F, Algaron F, Rizzello CG, Fox PF, Monnet V, Gobbetti M. 2003. Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides fromlactobacillus helveticusPR4 proteinase-hydrolyzed caseins of milk from six species. Appl Environ Microb 69:5297-305.
    • (2003) Appl Environ Microb , 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
  • 81
    • 0015368291 scopus 로고
    • Utilization of the iron of egg yolk for hemoglobin formation by the growing rat
    • Morris ER, Greene FE. 1972. Utilization of the iron of egg yolk for hemoglobin formation by the growing rat. J Nutr 702:901-8.
    • (1972) J Nutr , vol.702 , pp. 901-908
    • Morris, E.R.1    Greene, F.E.2
  • 82
    • 0000292126 scopus 로고    scopus 로고
    • Antioxidant activity of a Maillard-type phosvitin-galactomannan conjugate with emulsifying properties and heat stability
    • Nakamura S, Ogawa M, Nakai S, Kato A, Kitts DD. 1998. Antioxidant activity of a Maillard-type phosvitin-galactomannan conjugate with emulsifying properties and heat stability. J Agric Food Chem. 46:3958-63.
    • (1998) J Agric Food Chem , vol.46 , pp. 3958-3963
    • Nakamura, S.1    Ogawa, M.2    Nakai, S.3    Kato, A.4    Kitts, D.D.5
  • 83
    • 0032200879 scopus 로고    scopus 로고
    • S-casein and β-casein using immobilized glutamic acid-specific endopeptidase and characterization of their calcium binding
    • S-casein and β-casein using immobilized glutamic acid-specific endopeptidase and characterization of their calcium binding. J Dairy Sci 81:2858-65.
    • (1998) J Dairy Sci , vol.81 , pp. 2858-2865
    • Park, O.1    Allen, J.C.2
  • 84
    • 0023053348 scopus 로고
    • A Raman spectroscopic study of hen egg yolk phosvitin: structures in solution and in the solid state
    • Prescott B, Renugopalakrishnan V, Glimcher M J, Bhushan A, Thomas GJ Jr. 1986. A Raman spectroscopic study of hen egg yolk phosvitin: structures in solution and in the solid state. Biochem 25:2792-8.
    • (1986) Biochem , vol.25 , pp. 2792-2798
    • Prescott, B.1    Renugopalakrishnan, V.2    Glimcher, M.J.3    Bhushan, A.4    Thomas Jr, G.J.5
  • 85
    • 0022649985 scopus 로고
    • Bateriostatic activity of bovine milk lactoferrin against mastitic bacteria
    • Rainard P. 1986. Bateriostatic activity of bovine milk lactoferrin against mastitic bacteria. Vet Microbial 11:387-92.
    • (1986) Vet Microbial , vol.11 , pp. 387-392
    • Rainard, P.1
  • 86
    • 0022205442 scopus 로고
    • Structural studies of phosvitin in solution and in the solid state
    • Renugopalakrishnan V, Horowitz, PM, Glimcherg MJ. 1985. Structural studies of phosvitin in solution and in the solid state. J Biol Chem 260(21):11406-413.
    • (1985) J Biol Chem , vol.260 , Issue.21 , pp. 11406-11413
    • Renugopalakrishnan, V.1    Horowitz, P.M.2    Glimcherg, M.J.3
  • 87
    • 0031603296 scopus 로고    scopus 로고
    • Anticariogenic complexes of amorphous calcium phosphate stabilized by casein phosphopeptides. A review
    • Reynolds EC. 1998. Anticariogenic complexes of amorphous calcium phosphate stabilized by casein phosphopeptides. A review. Spec Care Dentist 18:8-16.
    • (1998) Spec Care Dentist , vol.18 , pp. 8-16
    • Reynolds, E.C.1
  • 88
    • 77952746207 scopus 로고    scopus 로고
    • Casein phosphopeptide-amorphous calcium phosphate: the scientific evidence
    • Reynolds EC. 2009. Casein phosphopeptide-amorphous calcium phosphate: the scientific evidence. Adv Dental Res 21:25-9.
    • (2009) Adv Dental Res , vol.21 , pp. 25-29
    • Reynolds, E.C.1
  • 89
    • 0035136024 scopus 로고    scopus 로고
    • Casein and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition
    • Rival SG, Boeriu CG, Wichers HJ. 2001b. Casein and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition. J Agric Food Chem 49:295-302.
    • (2001) J Agric Food Chem , vol.49 , pp. 295-302
    • Rival, S.G.1    Boeriu, C.G.2    Wichers, H.J.3
  • 90
    • 0035134979 scopus 로고    scopus 로고
    • Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties
    • Rival SG, Fornaroli S, Boeriu CG, Wichers HJ. 2001a. Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties. J Agric Food Chem 49:287-94.
    • (2001) J Agric Food Chem , vol.49 , pp. 287-294
    • Rival, S.G.1    Fornaroli, S.2    Boeriu, C.G.3    Wichers, H.J.4
  • 92
    • 20444369884 scopus 로고    scopus 로고
    • Induced resistance to the antimicrobial peptide lactoferrincin B inS. aureus.
    • Samuelsen O, Haukland HH, Jenssen H. 2005. Induced resistance to the antimicrobial peptide lactoferrincin B inS. aureus. FEBS Lett 579:3421-6.
    • (2005) FEBS Lett , vol.579 , pp. 3421-3426
    • Samuelsen, O.1    Haukland, H.H.2    Jenssen, H.3
  • 93
    • 0022668094 scopus 로고
    • Casein phosphopeptide (CPP) enhanced calcium absorption from the ligated segment of rat small intestine
    • Sato R, Noguchi T, Naito H. 1986. Casein phosphopeptide (CPP) enhanced calcium absorption from the ligated segment of rat small intestine. J Nutr Sci Vitaminol 32:67-76.
    • (1986) J Nutr Sci Vitaminol , vol.32 , pp. 67-76
    • Sato, R.1    Noguchi, T.2    Naito, H.3
  • 94
    • 0010766028 scopus 로고
    • The effect of feeding demineralized egg yolk protein on the solubility of intra-intestinal iron
    • Sato R, Noguchi T, Naito H. 1987. The effect of feeding demineralized egg yolk protein on the solubility of intra-intestinal iron. Nutr Rep Int 36:593-602.
    • (1987) Nutr Rep Int , vol.36 , pp. 593-602
    • Sato, R.1    Noguchi, T.2    Naito, H.3
  • 95
    • 33646518383 scopus 로고    scopus 로고
    • Antioxidant activity of white and black sesame seeds and their hull fractions
    • Shahidi F, Liyana-Pathirana CM, Wall DS. 2006. Antioxidant activity of white and black sesame seeds and their hull fractions. Food Chem 99:478-83.
    • (2006) Food Chem , vol.99 , pp. 478-483
    • Shahidi, F.1    Liyana-Pathirana, C.M.2    Wall, D.S.3
  • 97
    • 0015217461 scopus 로고
    • Phosvitin, a phosphjoglycoprotein
    • Shainkin R, Perlmann GE. 1971. Phosvitin, a phosphjoglycoprotein. J Biol Chem 240;2278-84.
    • (1971) J Biol Chem , vol.240 , pp. 2278-2284
    • Shainkin, R.1    Perlmann, G.E.2
  • 98
    • 0033828099 scopus 로고    scopus 로고
    • Bioactive peptides in dairy products: synthesis and interaction with proteolytic enzyme
    • Smacchi E, Gobbetti M. 2000. Bioactive peptides in dairy products: synthesis and interaction with proteolytic enzyme. Food Microbiol 17:129-41.
    • (2000) Food Microbiol , vol.17 , pp. 129-141
    • Smacchi, E.1    Gobbetti, M.2
  • 99
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • In Fox PF, editor. Vol London Elsevier Applied Science.
    • Swaisgood HE. 1992. Chemistry of the caseins. In Fox PF, editor. Advanced dairy chemistry. Vol 1 London Elsevier Applied Science. p 63-110.
    • (1992) Advanced dairy chemistry , vol.1 , pp. 63-110
    • Swaisgood, H.E.1
  • 100
    • 0014198147 scopus 로고
    • Phosvitin homogeneity and molecular weight
    • Taborsky G, Mok C. 1967. Phosvitin homogeneity and molecular weight. J Biol Chem 242:1495-501.
    • (1967) J Biol Chem , vol.242 , pp. 1495-1501
    • Taborsky, G.1    Mok, C.2
  • 101
    • 0942264735 scopus 로고
    • Interaction between phosvitin and iron and its effect on a rearrangement of phosvitin structure
    • Taborsky G. 1963. Interaction between phosvitin and iron and its effect on a rearrangement of phosvitin structure. Biochem 2:260-71.
    • (1963) Biochem , vol.2 , pp. 260-271
    • Taborsky, G.1
  • 102
    • 0014939155 scopus 로고
    • Effect of freezing and thawing on the conformation of phosvitin
    • Taborsky G. 1970. Effect of freezing and thawing on the conformation of phosvitin. J Biochem 245(5):1054-62.
    • (1970) J Biochem , vol.245 , Issue.5 , pp. 1054-1062
    • Taborsky, G.1
  • 103
    • 0015998078 scopus 로고
    • Phosphoproteins
    • Taborsky G. 1974. Phosphoproteins. Adv Prot Chem 28:1-210.
    • (1974) Adv Prot Chem , vol.28 , pp. 1-210
    • Taborsky, G.1
  • 104
    • 0018851918 scopus 로고
    • Iron binding by phosvitin and its conformational consequence
    • Taborsky G. 1980. Iron binding by phosvitin and its conformational consequence. J Biol Chem 255:2976-85.
    • (1980) J Biol Chem , vol.255 , pp. 2976-2985
    • Taborsky, G.1
  • 105
    • 0025950386 scopus 로고
    • On the interaction of phosvitins with ferric ion: solubility of the Fe(III)-phosphoprotein complex under acidic conditions is a function of the iron/phosphate ratio and the degree of phosvitin phosphorylation
    • Taborsky G. 1991. On the interaction of phosvitins with ferric ion: solubility of the Fe(III)-phosphoprotein complex under acidic conditions is a function of the iron/phosphate ratio and the degree of phosvitin phosphorylation. J Inorg Biochem 44:65-77.
    • (1991) J Inorg Biochem , vol.44 , pp. 65-77
    • Taborsky, G.1
  • 106
    • 84985204888 scopus 로고
    • Characterization of water soluble egg yolk proteins with isoelectric focusing
    • Ternes W. 1989. Characterization of water soluble egg yolk proteins with isoelectric focusing. J Food Sci 54:764-5.
    • (1989) J Food Sci , vol.54 , pp. 764-765
    • Ternes, W.1
  • 108
    • 74249109316 scopus 로고    scopus 로고
    • Casein phosphopeptide-amorphous calcium phosphate incorporated into sugar confections inhibits the progression of enamel subsurface lesions in situ
    • Walker GD, Cai F, Shen P, Adams GG, Reynolds C, Reynolds EC. 2010. Casein phosphopeptide-amorphous calcium phosphate incorporated into sugar confections inhibits the progression of enamel subsurface lesions in situ. Caries Res 44:33-40.
    • (2010) Caries Res , vol.44 , pp. 33-40
    • Walker, G.D.1    Cai, F.2    Shen, P.3    Adams, G.G.4    Reynolds, C.5    Reynolds, E.C.6
  • 109
    • 0022868429 scopus 로고
    • Chromatographic resolution of chicken phosvitin multiple macromolecular species in a classic viteliogenin-derived phosphoprotein
    • Wallace RA, Morgan JP. 1986. Chromatographic resolution of chicken phosvitin multiple macromolecular species in a classic viteliogenin-derived phosphoprotein. Biochem J 240:871-8.
    • (1986) Biochem J , vol.240 , pp. 871-878
    • Wallace, R.A.1    Morgan, J.P.2
  • 110
    • 0022163146 scopus 로고
    • Vitellogenesis and oocyte growth in nonmammalian vertebrates
    • In: Browder LW, editor. Vol, New York Plenum, p -
    • Wallace RA. 1985. Vitellogenesis and oocyte growth in nonmammalian vertebrates. In: Browder LW, editor. Developmental Biology. Vol 1, New York Plenum, p 127-77.
    • (1985) Developmental Biology , vol.1 , pp. 127-177
    • Wallace, R.A.1
  • 111
    • 0023731257 scopus 로고
    • New allergens from hen's egg white and egg yolk.In vitrostudy of ovomucin, apovitellenin I and VI, and phosvitin. Int Arch Allergy
    • Walsh BJ, Barnett D, Burley RW, Elliott C, Hill DJ, Howden ME. 1988. New allergens from hen's egg white and egg yolk.In vitrostudy of ovomucin, apovitellenin I and VI, and phosvitin. Int Arch Allergy Appl Immunol 87(1):81-6.
    • (1988) Appl Immunol , vol.87 , Issue.1 , pp. 81-86
    • Walsh, B.J.1    Barnett, D.2    Burley, R.W.3    Elliott, C.4    Hill, D.J.5    Howden, M.E.6
  • 112
    • 26944492664 scopus 로고    scopus 로고
    • Detection of four distinct groups of hen egg allergens binding IgE in the sera of children with egg allergy
    • Walsh BJ, Hill DJ, Macoun P, Cairns D, Howden ME. 2005. Detection of four distinct groups of hen egg allergens binding IgE in the sera of children with egg allergy. Allergol Immunopathol (Madr). 33(4):183-91.
    • (2005) Allergol Immunopathol (Madr) , vol.33 , Issue.4 , pp. 183-191
    • Walsh, B.J.1    Hill, D.J.2    Macoun, P.3    Cairns, D.4    Howden, M.E.5
  • 114
    • 0033866334 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibition: From viper to patient
    • Wimart MC, Komajda M. 2000. Angiotensin converting enzyme inhibition: From viper to patient. Heart 84:111-4.
    • (2000) Heart , vol.84 , pp. 111-114
    • Wimart, M.C.1    Komajda, M.2
  • 115
    • 0023942814 scopus 로고
    • Evolution of angiotensin-converting enzyme inhibitors
    • Wyvratt MJ. 1988. Evolution of angiotensin-converting enzyme inhibitors. Clin Physiol Bioch 6:217-9.
    • (1988) Clin Physiol Bioch , vol.6 , pp. 217-219
    • Wyvratt, M.J.1
  • 116
    • 35648935415 scopus 로고    scopus 로고
    • Antioxidant activity of tryptic digests of hen egg yolk phosvitin
    • Xu X, Katayama S, Mine Y. 2007. Antioxidant activity of tryptic digests of hen egg yolk phosvitin. J Sci Food Agric 87:2604-8.
    • (2007) J Sci Food Agric , vol.87 , pp. 2604-2608
    • Xu, X.1    Katayama, S.2    Mine, Y.3
  • 117
    • 0032901632 scopus 로고    scopus 로고
    • Ability of carnosine and other skeletal muscle components to quench unsaturated aldehydic lipid oxidation products
    • Zhou S, Decker EA. 1999a. Ability of carnosine and other skeletal muscle components to quench unsaturated aldehydic lipid oxidation products. J Agric Food Chem 47:51-5.
    • (1999) J Agric Food Chem , vol.47 , pp. 51-55
    • Zhou, S.1    Decker, E.A.2
  • 118
    • 0032819575 scopus 로고    scopus 로고
    • Ability of amino acids, dipeptides, polyamines, and sulfhydryls to quench hexanal, a saturated aldehydic lipid oxidation product
    • Zhou S, Decker EA. 1999b. Ability of amino acids, dipeptides, polyamines, and sulfhydryls to quench hexanal, a saturated aldehydic lipid oxidation product. J Agric Food Chem 47:1932-6.
    • (1999) J Agric Food Chem , vol.47 , pp. 1932-1936
    • Zhou, S.1    Decker, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.