Inhibition of human lymphocyte transformation by human. cap alpha. -fetoprotein (HAFP) [electronic resource] : studies on the mode of HAFP action and the role of HAFP polymorphism
- Washington, D.C. : United States. Dept. of Energy, 1977.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
- Physical Description:
- Pages: 22 : digital, PDF file
- Additional Creators:
- United States. Department of Energy
United States. Department of Energy. Office of Scientific and Technical Information
- 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.
- Published through SciTech Connect.
5. meeting of the international research group for carcino embryonic proteins, Copenhagen, Denmark, 6 Aug 1977.
Miller, J. B.; Yachnin, S.; Lester, E. P.
Chicago Univ., Ill. (USA). Dept. of Medicine
Franklin McLean Memorial Research Inst., Chicago, Ill. (USA)
- Funding Information:
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