SULFATION OF PROTEINS IN THE PRIMATE CEREBELLUM AND YOUNG-RAT BRAIN

Protein tyrosine sulfotransferase activity in a 20,000 g sedimentable fraction of monkey cerebellum was demonstrated. Both endogenous protei ns and the exogenous substrate poly (Glu, Ala, Tyr) random copolymer w ere sulfated. The copolymer in the low molecular mass range (approx 20 kDa) was preferentially sulfated. Addition of copolymer inhibited sul fation of endogenous proteins. Mg2+ and Mn2+ promoted sulfation. S-35- Labeled proteins from monkey cerebellum and young (10 days old) rat br ain 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 Ri cinus Communis agglutinin-Sepharose column suggesting the presence of mannose or galactose containing glycosulfoproteins.