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Inhibition of human lymphocyte transformation by human. cap alpha. -fetoprotein (HAFP): studies on the mode of HAFP action and the role of HAFP polymorphism

Conference ·
OSTI ID:7291187
To explain the mechanism of inhibition of human lymphocyte transformation by human alpha-fetoprotein (HAFP), we sought for, and failed to find, evidence of physical association between HAFP and phytomitogens or antihuman thymocyte antiserum. In addition, 20 to 40 fold increases in mitogen dose do not reverse the inhibition of lymphocyte transformation by a constant dose of HAFP. The presence of HAFP does not interfere with the attachment of /sup 125/I-labeled phytohemagglutinin to the lymphocyte surface. Two-dimensional crossed immunoelectrophoresis of HAFP isolated from the body fluids of hepatoma patients demonstrates three charged species of HAFP designated as HAFP-1 (the most cathodal), HAFP-2, and HAFP-3 (the most anodal). The potency of HAFP isolates in inhibiting lymphocyte transformation can be positively correlated with the ratio HAFP-3 : HAFP-1 in each preparation. Passage of HAFP isolates over CM-cellulose allows the isolation of two HAFP fractions, one at pH 4.95, and the other at pH 5.24. The pH 4.95 CM-cellulose isolate is enriched in the more electronegative HAFP species (HAFP-3) and is, on the average, two times more potent than the pH 5.24 CM-cellulose HAFP isolate. The latter, by comparison with native HAFP, is enriched in the more electropositive HAFP species (HAFP-1). The CM-cellulose HAFP isolates are identical in sialic acid content.
Research Organization:
Chicago Univ., Ill. (USA). Dept. of Medicine; Franklin McLean Memorial Research Inst., Chicago, Ill. (USA)
Sponsoring Organization:
USDOE
OSTI ID:
7291187
Report Number(s):
CONF-770860-2
Country of Publication:
United States
Language:
English