Abstract
Protein tyrosine sulfotransferase activity in a 20,000 g sedimentable fraction of monkey cerebellum was demonstrated. Both endogenous proteins and the exogenous substrate poly (Glu, Ala, Tyr) random copolymer were sulfated. The copolymer in the low molecular mass range (approx 20 kDa) was preferentially sulfated. Addition of copolymer inhibited sulfation of endogenous proteins. Mg 2+ and Mn 2+ promoted sulfation. 35S-Labeled proteins from monkey cerebellum and young (10 days old) rat brain were subjected to lectin-Sepharose chromatography to identify the presence of sulfated glyco-proteins. Labeled proteins from both these sources could bind and get eluted from Concanavalin A-Sepharose and Ricinus Communis agglutinin-Sepharose column suggesting the presence of mannose or galactose containing glycosulfoproteins.
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