SEROLOGICAL STUDIES ON HEAT-INDUCED INTERACTIONS OF ALPHA-LACTALBUMIN AND MILK-PROTEINS

被引：42

作者：

BAER, A ^{[1
]}

OROZ, M ^{[1
]}

BLANC, B ^{[1
]}

机构：

[1] FED DAIRY RES INST, CH-3097 LIEBEFELD, SWITZERLAND

来源：

JOURNAL OF DAIRY RESEARCH | 1976年 / 43卷 / 03期

关键词：

D O I：

10.1017/S0022029900016009

中图分类号：

S8 [畜牧、动物医学、狩猎、蚕、蜂];

学科分类号：

0905 ;

摘要：

The heat denaturation of .alpha.-lactalbumin (.alpha.-la) in NaCl and KCl solutions, [cow] milk ultrafiltrate and milk was studied using the method of micro complement fixation. This protein was very resistant to heat denaturation and it was more stable in milk ultrafiltrate than in the other media studied at temperatures up to 70.degree. C. Of the various milk proteins added to .alpha.-la, only .beta.-lactoglobulin (.beta.-lg) formed a heat-induced complex with this protein. This complex was identical in milk ultrafiltrate or in milk and depended on the molar ratio between both proteins; it was not modified by any other milk proteins. The binding of .alpha.-la to .beta.-lg changed the ability of the latter protein to bind .kappa.-casein.

引用

页码：419 / 432

页数：14

共 18 条

[1]

[Anonymous], 1967, HDB EXPT IMMUNOLOGY

[2]

ARMSTRONG JM, 1970, BIOCHIM BIOPHYS ACTA, V214, P419

[3]

BREW K, 1967, J BIOL CHEM, V242, P3747

[4] ETUDE DUNE ETAPE REVERSIBLE DANS LA THERMODENATURATION DE LA BETA-LACTOGLOBULINE BOVINE A [J].