Identification and isolation of an agglutinin from uterus of rats

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 agglutin is Ca ++ dependent, a glycoprotein, and composed of two very closely associated bands of molecular weights 28,000 and 30...

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Veröffentlicht in:Biochemical and biophysical research communications 1985-08, Vol.130 (3), p.1301-1307
Hauptverfasser: Chowdhury, Mridula, Sarkar, Manju, Mandal, Chitra
Format: Artikel
Sprache:eng
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Zusammenfassung: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 agglutin 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.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(85)91756-5