Antigenicity of a new diethylnitrosamine-induced transplantable guinea pig hepatoma: pathology and formation of ascites variant.
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Biomedical subjects
Publications and source records attributed to T Borsos.
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With the use of the first component of guinea pig complement (C'1) labeled in vivo with (14)C-amino acids, we have obtained evidence that, under the conditions required for the assay of C'1, each molecule of C'1 capable of interaction with cell surface antigen-antibody complexes is capable of initiating the reaction sequence that leads to lysis of the cell.
The titer of late-acting complement components in sera from male mice is 8-10 times higher than the titer of sera from female mice. Using assays developed to measure the serum content of two of the late-acting components, we have shown that this difference is due to the effect of androgen and estrogen on these two late-acting complement components. These two components have been tentatively identified as C'5 and C'6. Androgen and estrogen have greater effect on C'6 than on C'5. The possibility has not been excluded that still other of the late-acting complement components are affected by androgens and estrogens. The course of homograft rejection was unchanged in mice deficient in C'5 and C'6.
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The mechanism of complement fixation on cell surfaces by whole antiserums, and by 19S and 7S fractions has been studied with a new comple-ment-fixation test. This test is based on the fixation and transfer of the activated first component of complement (C1a). We have concluded that a single molecule of 19S antibody in combination with antigen at the cell surface is sufficient to bind one molecule of C1a. For 7S antibodies at least two molecules in close proximity at the cell surface are required to fix one molecule of C1a.
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