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.