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- W1671711700 abstract "Publisher Summary This chapter discusses the method of assay and purification of the sulfotransferases responsible for the sulfation of chondroitin sulfates and heparitin sulfate. Sulfates (S) are transferred to unsulfated acetylhexosamine residues with the formation of acetylhexosamine monosulfate resiclues or they are transferred to hexosamine monosulfate residues with the formation of acetylhexosamine disulfate residues. Enzyme fractionation and the study of acceptor specificity show that separate enzymes (sulfotransferases) are involved in the addition of sulfate to chondroitin sulfates A, B, or C, heparitin sulfate, and heparin. The assay depends on measurement of incorporation of 35S from 3′-phosphoadenosine 5′-phosphosulfate (PAP35S) into mucopolysaccharides. The technique is based on the paper chromatographic immobility of mucopolysaccharides in appropriate solvents, PAP35S, AP35S, inorganic 35S-sulfate, and other low molecular weight 35S-products of enzymatic activity move down the paper in this system. The assay requires the availability of PAP35S. A specific heparitin sulfate sulfotransferase is purified from the crude extract by chromatography on diethylaminoethyl (DEAE)-cellulose column, suggesting that the crude enzyme preparation might contain several sulfotransferases, each specific for a particular acceptor." @default.
- W1671711700 created "2016-06-24" @default.
- W1671711700 creator A5005424255 @default.
- W1671711700 date "1966-01-01" @default.
- W1671711700 modified "2023-09-26" @default.
- W1671711700 title "[85] Sulfation of mucopolysaccharides by enzymes from hen oviduct" @default.
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- W1671711700 doi "https://doi.org/10.1016/0076-6879(66)08090-x" @default.
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