Oestrone binding properties of nine molecular variants of rat alpha-foetoprotein.
Rat alpha-foetoprotein was separated into nine molecular variants by electrophoresis and affinity chromatography on Ricinus communis agglutinin and concanavalin-A. The nine variants are able to bind oestrone with the same capacity of one binding site per alpha-foetoprotein molecule. The association constants seem to vary with the sialic acid composition of the iso-alpha-foetoprotein.
D000653:Amniotic Fluid / Q000378:metabolism; D000818:Animals; D002846:Chromatography, Affinity; D004970:Estrone / Q000378:metabolism*; D005260:Female; D007700:Kinetics; D037102:Lectins; D008970:Molecular Weight; D011247:Pregnancy; D051381:Rats; D000509:alpha-Fetoproteins / Q000302:isolation & purification / Q000378:metabolism*
D037102:Lectins; D000509:alpha-Fetoproteins; D004970:Estrone