STRUCTURE OF THE GLYCAN CHAIN FROM THE SURFACE-LAYER GLYCOPROTEIN OF CLOSTRIDIUM-THERMOHYDROSULFURICUM L77-66

被引:14
作者
ALTMAN, E
BRISSON, JR
GAGNE, SM
KOLBE, J
MESSNER, P
SLEYTR, UB
机构
[1] AGR UNIV VIENNA,ZENTRUM ULTRASTRUKTFORSCH,A-1180 VIENNA,AUSTRIA
[2] AGR UNIV VIENNA,LUDWIG BOLTZMANN INST MOLEK NANOTECHNOL,A-1180 VIENNA,AUSTRIA
关键词
GLYCAN; GLYCAN STRUCTURE; COSY; NOESY; SURFACE LAYER GLYCOPROTEIN; S-LAYER;
D O I
10.1016/0304-4165(92)90164-P
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
The thermophilic eubacterium Clostridium thermohydrosulfuricum L77-66 is covered by a crystalline surface layer composed of identical glycoprotein subunits which are arranged in a hexagonal lattice with centre-to-centre spacings of approx. 14.3 nm. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of cell wall preparations showed the presence of several broadened, carbohydrate-containing bands in a molecular mass range of 90 to 200 kDa. A total carbohydrate content of approx. 14% was determined in the purified surface layer glycoprotein. Chemical deglycosylation of this material by trifluoromethanesulfonic acid resulted in the disappearance of the complex banding pattern. Only a single band with a molecular mass of 82 kDa remained visible upon Coomassie staining. After proteolytic digestion of the surface layer glycoprotein a single glycopeptide fraction with an apparent molecular mass of approx. 25 kDa was obtained by gel filtration. Composition analysis, methylation, periodate oxidation and a combination of homonuclear and H-1-detected heteronuclear shift-correlated nuclear magnetic resonance experiments established the following structure for the glycan chain of the surface layer glycoprotein: [GRAPHICS]
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收藏
页码:71 / 77
页数:7
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