Biological and biochemical properties of Nonidet P40-solubilized and partially purified tumor-specific antigens of the transplantation type from plasma membranes of a methylcholanthrene-induced sarcoma

Natori, T.; Law, L.W.; Appella, E.

Cancer Research 37(9): 3406-3413

1977


ISSN/ISBN: 0008-5472
PMID: 69494
Document Number: 112774
Tumor-specific transplantation antigen (TSTA) was solubilized from cell membranes of with nonionic detergent Nonidet P40. Soluble TSTA was partially characterized by chromatographic separation and electrophoresis. The antigen responsible for tumor rejection activity had a MW of approximately 70,000 daltons in the presence of detergent and an electrophoretic mobility of .alpha.-globulin. TSTA was well separated from mouse histocompatibility antigen H-2 by lectin affinity chromatography. The antigen purified by a sequence of procedures, including gel filtration, lectin affinity chromatography, column electrophoresis, and rechromatography on agarose, showed only 3 major bands on polyacrylamide gel electrophoresis. TSTA was specific for sarcoma Meth-A.

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