참고문헌
- Int J Dairy Technol v.54 Milk proteins as food ingredients Fox,P.F. https://doi.org/10.1046/j.1471-0307.2001.00014.x
- Crit Re Food Sci Nutr v.36 Structures and functionalities of milk proteins Wong,D.W.S.;Cairand,W.M.;Paviath,A.E. https://doi.org/10.1080/10408399609527751
- Dairy Chemistry and Biochemistry Fox,P.F.;McSweeney,P.L.H.
- Food Technol v.30 Whey protein concentrates : an update Morr,C.V.
- J Dairy Res v.44 A calorimetric study of thermal denaturation of whey protein in simulated milk ultrafiltrate Ruegg,M.;Moor,U.;Blanc,B. https://doi.org/10.1017/S002202990002046X
- Neth Milk Dairy J v.37 Evaluation of functional properties of whey protein concentrates and whey protein isolates de Wit,J.N.;Klarenbeck,G.;Hontelez Backx,E.
- J Dairy Sci v.67 Effect of calcium binding on thermal denaturation of bovine α-lactalbumin Bernal,V.;Jelen,P. https://doi.org/10.3168/jds.S0022-0302(84)81595-7
- J Dairy Res v.53 Irreversible heat denaturation of bovine a-lactalbumin Chaplin,L.C.;Lyster,R.L.J. https://doi.org/10.1017/S0022029900024857
- Biochim Biophys Res Commun v.95 α-Lactalbumin: a calcium metalloprotein Hiraoka,Y.;Segawa,T.;Kuwajima,K.;Sugai,S.;Murai,N. https://doi.org/10.1016/0006-291X(80)91585-5
- Developments in dairy chemistry-4 The milk protein system Fox,P.F.
- J Dairy Sci v.67 Nomenclature of proteins of cows milk; fifth revision Eigel,W.N.;Butler,J.E.;Ernstrom,C.A.;Farrel Jr,H.M.;Harwalker,V.R.;Jenness,R;Whitney,R.M. https://doi.org/10.3168/jds.S0022-0302(84)81485-X
- Dairy Industry and Technol v.1 Milk, the rich source of bioreactive-ingredients for functional nutraceutical and pharmaceutical industry Ha,E.Y.W.
-
Biochemical J
v.220
High-affinity binding of
$Ca^{2+}$ to bovine α-lactalbumin in the asbsence and presence Bryant,D.T.W.;Andrews,P. - J Dairy Sci v.76 Effect of sodium and calcium additionon thermal denaturation of apo-α-lactalbumin: a differential scanning calorimetric study Relikin,P.;Launay,B.;Eynard,L. https://doi.org/10.3168/jds.S0022-0302(93)77321-X
- Crit Rev Food Sci Nutr v.36 Thermal unfolding of β-lactoglobulin, α-lactalbumin, and bovine serum albumin. A thermodynamic approach Relkin,P. https://doi.org/10.1080/10408399609527740
- J Dairy Res v.65 Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions Havea,P.;Singh,H.;Creamer,L.K.;Campanella,O. https://doi.org/10.1017/S0022029997002641
- J Dairy Res v.50 Proteinase in normal bovine milk and their action on casein Andrews,A.T. https://doi.org/10.1017/S0022029900032519
- Nature v.227 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Laemmli,U.K. https://doi.org/10.1038/227680a0
- J. Agric Food Chem v.46 Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A,B and C Manderson,G.A.;Hardman,M.J.;Creamer,L.K. https://doi.org/10.1021/jf980515y
- Biochem Biophys Res Comm v.157 The calcium-dependent electrophoretic shift of a-lactalbumin, the modifier protein of galactosyl transferase Thompson,M.P.;Groves,M.L.;Brower,D.P.;Farrell,H.M.;Jenness,R.;Kotts,C.E. https://doi.org/10.1016/S0006-291X(88)80965-3
- Food Chem v.52 A three-state heat-denaturation of bovine α-lactalbumin Apenten,R.K.O. https://doi.org/10.1016/0308-8146(94)P4191-H
- FEBS Letters v.473 a-Lactalbumin: structure and function Permyakov,E.A.;Berliner,L.J. https://doi.org/10.1016/S0014-5793(00)01546-5
- Int Dairy J v.13 Changed protein structures of bovine β-lactoglobulin and α-lactalbumin as a consequence of heat treatment Hong,Y.H.;Creamer,L.K.
- J Dairy Res v.68 Characterization of heat-induced aggregates of β-lactoglobulin and α-lactalbumin and bovine serum albumin in a whey protein concentrate environment Havea,P.;Singh,H.;Creamer,L.K.
피인용 문헌
- Electrophoretic Behaviors of α-Lactalbumin and β-Lactoglobulin Mixtures Caused by Heat Treatment vol.16, pp.7, 2002, https://doi.org/10.5713/ajas.2003.1041