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J. Biol. Chem., Vol. 269, Issue 40, 24538-24541, Oct, 1994
H Wlad, M Maccarana, I Eriksson, L Kjellen and U Lindahl
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 of 35S from 3'-phosphoadenosyl-5'-phospho-[35S]sulfate into
N,O-desulfated, re-N-sulfated heparin. Anion-exchange high performance
liquid chromatography of disaccharides obtained by deaminative cleavage of
the 35S-labeled polysaccharide product revealed O-35S-sulfation at C-2 of
L-iduronic acid and at C-6 of D-glucosamine units. SDS-polyacrylamide gel
electrophoresis of semipurified enzyme followed by extraction of gel
segments and renaturation of proteins consistently showed two distinct
fractions of O-sulfotransferase activity, corresponding to proteins of
approximately 20 and approximately 60 kDa. The approximately 60-kDa
enzyme(s) catalyzed both the 2-O- and 6-O-sulfotransferase reactions,
whereas the approximately 20-kDa fraction promoted iduronosyl 2-O-sulfation
only. These results are discussed in relation to previous findings,
indicating that some of the enzymes involved in heparin biosynthesis
catalyze more than one reaction.
Biosynthesis of heparin. Different molecular forms of O- sulfotransferases
Department of Medical and Physiological Chemistry, Uppsala University, Sweden.
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