A BOVINE IGG HEAVY-CHAIN CONTAINS N-ACETYLGALACTOSAMINYLATED N-LINKED SUGAR CHAINS

被引：9

作者：

AOKI, N

FURUKAWA, K

IWATSUKI, K

NODA, A

SATO, T

NAKAMURA, R

MATSUDA, T

机构：

[1] NAGOYA UNIV,SCH AGR SCI,DEPT APPL BIOL SCI,NAGOYA,AICHI 46401,JAPAN

[2] TOKYO METROPOLITAN GERIATR HOSP & INST GERENTOL,DEPT BIOSIGNAL RES,ITABASHI KU,TOKYO 173,JAPAN

[3] UNIV TOKYO,INST MED SCI,DEPT BIOCHEM,TOKYO 108,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 210卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1657

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 56K protein co-purified with bovine milk fat globule membrane (MF-GM) proteins bound to Wisteria floribunda agglutinin (WFA) like most MFGM glycoproteins. Treatment with N-glycanase or beta-N-acetylhexosaminidase abolished the lectin binding to the protein. Amino acid sequence and immunoblot analyses revealed that the 56K protein is an IgG heavy chain. Lectin column chromatography of the oligosaccharides released by hydrazinolysis from the purified IgG heavy chains revealed that 0.08% of the total N-linked sugar chains bind to a WFA-agarose column, suggesting that they contain the beta-N-acetylgalactosaminylated structure. (C) 1995 Academic Press, Inc.

引用

页码：275 / 280

页数：6

共 23 条

[1] COPURIFICATION OF BOVINE-MILK XANTHINE-OXIDASE AND IMMUNOGLOBULIN [J].