SITE-SPECIFIC AND COMPLETE ENZYMATIC DEGLYCOSYLATION OF THE NATIVE HUMAN CHORIONIC-GONADOTROPIN ALPHA-SUBUNIT

被引：0
|
作者：
VANZUYLEN, CWEM
DEBEER, T
RADEMAKER, GJ
HAVERKAMP, J
THOMASOATES, JE
HARD, K
KAMERLING, JP
VLIEGENTHART, JFG
机构：
[1] UNIV UTRECHT,BIJVOET CTR,DEPT BIOORGAN CHEM,3508 TB UTRECHT,NETHERLANDS
[2] UNIV UTRECHT,BIJVOET CTR,DEPT MASS SPECTROMETRY,3508 TB UTRECHT,NETHERLANDS
[3] UNIV UTRECHT,BIJVOET CTR,DEPT NMR SPECTROSCOPY,3508 TB UTRECHT,NETHERLANDS
[4] UNIV UTRECHT,SON NMR LARGE SCALE FACIL,UTRECHT,NETHERLANDS
来源：
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1995年 / 231卷 / 03期
关键词：
GLYCOPROTEIN; HUMAN CHORIONIC GONADOTROPIN; SITE-SPECIFIC N-DEGLYCOSYLATION;
D O I：
暂无
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：
Numerous studies have shown that glycosylation of the alpha-subunit of human chorionic gonadotropin (alpha hCG) is essential for the biological activity of this hormone. To obtain detailed insight into the function of N-glycosylation, the availability of site-specifically and fully deglycosylated alpha-subunits obtained under non-denaturing conditions is a prerequisite. NMR spectroscopy in combination with FAB-mapping demonstrates that only Asn52 of the alpha-subunit is accessible to digestion by peptide-N-4-(N-acetyl-beta-glucosaminyl)asparagine amidase F under native conditions. Treatment of native alpha hCG with endo-beta-N-acetylglucosaminidase B results in full deglycosylation yielding alpha hCG with one GlcNAc residue at both Asn52 and Asn78.
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页码：754 / 760
页数：7
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