CHEMICAL CHARACTERIZATION OF THE REGULARLY ARRANGED SURFACE-LAYER GLYCOPROTEIN OF CLOSTRIDIUM-THERMOSACCHAROLYTICUM D120-70

被引:22
作者
ALTMAN, E
BRISSON, JR
MESSNER, P
SLEYTR, UB
机构
[1] AGR UNIV VIENNA,ZENTRUM ULTRASTRUKT FORSCH,A-1180 VIENNA,AUSTRIA
[2] AGR UNIV VIENNA,LUDWIG BOLTZMANN INST ULTRASTRUKT FORSCH,A-1180 VIENNA,AUSTRIA
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 188卷 / 01期
关键词
D O I
10.1111/j.1432-1033.1990.tb15373.x
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
Clostridium thermosaccharolyticum D120‐70 possesses as its outermost cell envelope layer a square‐arranged array of glycoprotein molecules. SDS/polyacrylamide gel electrophoresis of the purified surface layer showed a broadened band in the molecular mass range of about 115 kDa which, upon periodic acid/Schiff staining, gave a positive reaction. After proteolytic degradation of this material, two glycopeptide fractions were obtained. One‐and two‐dimensional nuclear magnetic resonance studies, together with methylation analysis and periodate oxidation, were used to determine the structures of the polysaccharide portions of these glycopeptides. The combined chemical and spectroscopic evidence suggests the following structures: (Formula Presented.) Copyright © 1990, Wiley Blackwell. All rights reserved
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收藏
页码:73 / 82
页数:10
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