Further resolution of human alpha-fetoprotein by affinity electrophoresis with erythroagglutinating phytohemagglutinin of Phaseolus vulgaris lectin

Taketa, K.; Ichikawa, E.; Nakabayashi, H.; Sato, J.; Kato, K.; Akai, S.; Ohkawa, R.; Ohkawa, K.; Taga, H.; Hirai, H.

Tumour Biology the Journal of the International Society for Oncodevelopmental Biology and Medicine 6(6): 519-531

1985


ISSN/ISBN: 1010-4283
PMID: 2426755
Accession: 040187270

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Abstract
Major molecular species of human alpha-fetoprotein(AFP), which were separated as single components by serial affinity chromatography with concanavalin A(Con-A) and Lens culinaris agglutinin, were further resolved into several bands by affinity electrophoresis with erythroagglutinating phytohemagglutinin of Phaseolus vulgaris lectin(E-PHA). Among the newly separated main molecular species, both Con-A- and E-PHA-reactive AFP(AFP-1X1) was demonstrated, contrary to the known sugar specificity of Con-A and E-PHA, in addition to molecular species of AFP reacting with Con-A but not with E-PHA(AFP-1X0) and of AFP reacting with E-PHA but not with Con-A(AFP-0X1). AFP-0X1 was formed from AFP-0X0, and AFP-1X1 from AFP-1X0 by neuraminidase treatment; thus, AFP-0X1 and AFP-1X1 represent asialylated and AFP-0X0 and AFP-1X0 sialylated molecular species. AFP-1X1' and AFP-0X0' were present as minor components. AFP-0X0' had no affinity for E-PHA, and the affinity increased in the order of AFP's-0X0(or 0X1), -1X1', -1X1 and -0X1. Proportions of those components varied depending on the pathophysiological conditions of AFP production.