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 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.
M
M
Chowdhury
M
M
Sarkar
C
C
Mandal
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D004971:Estrus; D005260:Female; D006023:Glycoproteins; D006384:Hemagglutination; D037102:Lectins / Q000302:isolation & purification*; D008970:Molecular Weight; D009844:Oligosaccharides; D011247:Pregnancy; D051381:Rats; D012794:Sialic Acids; D014599:Uterus / Q000032:analysis*; D000509:alpha-Fetoproteins
D006023:Glycoproteins; D037102:Lectins; D009844:Oligosaccharides; D012794:Sialic Acids; D000509:alpha-Fetoproteins