HOMOGENEITY OF SULFHYDRYL OXIDASE PREPARATIONS OBTAINED BY TRANSIENT COVALENT AFFINITY-CHROMATOGRAPHY

被引：4

作者：

JANOLINO, VG

SWAISGOOD, HE

机构：

[1] Department of Food Science, Southeast Dairy Foods Research Center, North Carolina State University, Raleigh

来源：

JOURNAL OF DAIRY SCIENCE | 1990年 / 73卷 / 02期

关键词：

covalent affinity chromatography; immunoglobulin; sulfhydryl oxidase;

D O I：

10.3168/jds.S0022-0302(90)78674-2

中图分类号：

S8 [畜牧、动物医学、狩猎、蚕、蜂];

学科分类号：

0905 ;

摘要：

Bovine milk sulfhydryl oxidase was prepared by transient covalent affinity chromatography on a cysteinylsuccinamidopropyl glass matrix. The homogeneity of this preparation was examined by immunofixation electrofocusing, SDS-PAGE, and size exclusion chromatography in 6 M guanidinium chloride. The major contaminant of this preparation, prepared from whey diafiltered with a 1000 kdal exclusion limit membrane, was IgG. Immunoglobulin M could not be detected. Presence of IgG in these sulfhydryl oxidase preparations suggests an interaction between IgG and either skim milk membrane vesicles or sulfhydryl oxidase. © 1990, American Dairy Science Association. All rights reserved.

引用

页码：308 / 313

页数：6

共 13 条

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