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Sulfation of proteins in the primate cerebellum and young rat brain.

Authors
  • Rao, A S
  • Cherian, R
  • Balasubramanian, A S
Type
Published Article
Journal
Neurochemistry International
Publisher
Elsevier
Publication Date
May 01, 1993
Volume
22
Issue
5
Pages
465–470
Identifiers
PMID: 8485452
Source
Medline
License
Unknown

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.

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