title: Sulfation of proteins in the primate cerebellum and young rat brain.
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. Mg2+ and Mn2+ 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.
authors: Department of Neurological Sciences, Christian Medical College & Hospital, Vellore, India.
authors: A S
authors: AS
authors: Rao
authors: R
authors: R
authors: Cherian
authors: A S
authors: AS
authors: Balasubramanian
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D002531:Cerebellum / Q000201:enzymology*; D002845:Chromatography; D005690:Galactose / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis / Q000378:metabolism; D008255:Macaca radiata; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008358:Mannose / Q000032:analysis; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D051381:Rats; D012965:Sodium Chloride / Q000494:pharmacology; D013379:Substrate Specificity; D013431:Sulfates / Q000378:metabolism*; D015238:Sulfotransferases / Q000037:antagonists & inhibitors / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D009419:Nerve Tissue Proteins; D013431:Sulfates; D008345:Manganese; D012965:Sodium Chloride; D015238:Sulfotransferases; C039079:protein-tyrosine sulfotransferase; D008274:Magnesium; D008358:Mannose; D005690:Galactose