Biosynthesis of heparin. Different molecular forms of O-sulfotransferases.
作者： U Lindahl , L Kjellén , I Eriksson , M Maccarana , H Wlad
DOI: 10.1016/S0021-9258(17)31423-0
关键词:
摘要: O-Sulfotransferases involved in heparin biosynthesis were purified > or = 10,000-fold from detergent extracts of mouse mastocytoma tissue by sequential chromatographies on DEAE-Sephacel, heparin-agarose, blue Sepharose, and 3',5'-ADP-Sepharose. The resultant preparation catalyzed the transfer 35S 3'-phosphoadenosyl-5'-phospho-[35S]sulfate into N,O-desulfated, re-N-sulfated heparin. Anion-exchange high performance liquid chromatography disaccharides obtained deaminative cleavage 35S-labeled polysaccharide product revealed O-35S-sulfation at C-2 L-iduronic acid C-6 D-glucosamine units. SDS-polyacrylamide gel electrophoresis semipurified enzyme followed extraction segments renaturation proteins consistently showed two distinct fractions O-sulfotransferase activity, corresponding to approximately 20 60 kDa. 60-kDa enzyme(s) both 2-O- 6-O-sulfotransferase reactions, whereas 20-kDa fraction promoted iduronosyl 2-O-sulfation only. These results are discussed relation previous findings, indicating that some enzymes catalyze more than one reaction.
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