MICROHETEROGENEITY OF A PURIFIED IGG1 DUE TO ASYMMETRIC FAB GLYCOSYLATION

被引：20

作者：

GREBENAU, RC ^{[1
]}

GOLDENBERG, DM ^{[1
]}

CHANG, CH ^{[1
]}

KOCH, GA ^{[1
]}

GOLD, DV ^{[1
]}

KUNZ, A ^{[1
]}

HANSEN, HJ ^{[1
]}

机构：

[1] CTR MOLEC MED & IMMUNOL,NEWARK,NJ 07103

来源：

MOLECULAR IMMUNOLOGY | 1992年 / 29卷 / 06期

关键词：

D O I：

10.1016/0161-5890(92)90185-Z

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A murine monoclonal anti-granulocyte IgG1, IMMU-MN3. was seen to exhibit heterogeneity. On reduced SDS-PAGE, the purified antibody appeared as two heavy-chain bands of unequal intensity, and only one light-chain band. Hydrophobic interaction chromatography (HIC) also resolved two Populations of the IMMU-MN3 antibody. Based on Concanavalin A affinity chromatography, enzymatic digestion with Endoglycosidase F and carbohydrate analysis, it was found that the heterogeneity detected by SDS-PAGE and HIC was due to differences in glycosylation. Furthermore. sequential gel analysis (non-reduced/reduced) demonstrated that the upper heavy-chain band was asymmetrically glycosylated.

引用

页码：751 / 758

页数：8

共 37 条

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