Aussel C, Kerckaert J P, Bayard B
Biochim Biophys Acta. 1978 Apr 26;533(2):504-10. doi: 10.1016/0005-2795(78)90396-3.
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.
通过电泳以及在蓖麻凝集素和伴刀豆球蛋白A上进行亲和层析，大鼠甲胎蛋白被分离为9种分子变体。这9种变体能够以每个甲胎蛋白分子一个结合位点的相同能力结合雌酮。缔合常数似乎随同种甲胎蛋白的唾液酸组成而变化。
