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 |
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Hauptverfasser: | , , |
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. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(85)91756-5 |