| Literature DB >> 2411268 |
M Chowdhury, M Sarkar, C Mandal.
Abstract
A sialic acid-binding agglutinin was purified to apparent homogeneity by affinity chromatography on fetuin-sepharose column from the rat uterine homogenate in estrus. The agglutinin is Ca++ dependent, a glycoprotein, and composed of two very closely associated bands of molecular weights 28,000 and 30,000 and pIs of 4 and 4.1. Several sialoglycoproteins, sialic acid, EDTA, glucuronic acid and heparin acted as an inhibitor of the agglutinin.Entities:
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Year: 1985 PMID: 2411268 DOI: 10.1016/0006-291x(85)91756-5
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575