COMPARISON OF THE BINDING OF RADIOLABELED HUMAN-IGG AND FC FRAGMENTS TO MURINE SPLEEN-CELLS
COMPARISON OF THE BINDING OF RADIOLABELED HUMAN-IGG AND FC FRAGMENTS TO MURINE SPLEEN-CELLS
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DOI:
10.1111/j.1365-3083.1979.tb01368.x
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发表时间:
1979-01-01
影响因子:
3.7
通讯作者:
WEIGLE, WO
中科院分区:
文献类型:
--
作者:
MORGAN, EL;SPIEGELBERG, HL;WEIGLE, WO
Binding properties of an Ig[immunoglobulin]G1 human myeloma protein, normal IgG, and the Fc and Fab fragments of each were compared in cultures of murine spleen cells. Both 125I-labeled IgG and Fc fragments bound to splenic lymphocytes, whereas Fab fragments did not bind significantly at the highest concentrations tested. On a molar basis, more Fc bound than intact IgG. According to Scatchard plot analysis, the affinity constant of IgG1 was 1.5 .times. 106 .+-. 1 .times. 105 l/M [molecules] and that of the Fc fragments was 7.8 .times. 105 .+-. 2.6 .times. 105 l/M. Approximately 25,000 binding sites/cell were calculated for IgG1 and 102,000 for Fc. Deaggregation of the Fc preparation did not change these values, suggesting that the difference in binding of IgG and Fc did not result from Fc aggregation. Unlabeled IgG inhibited about 25% of the labeled Fc binding, whereas unlabeled Fc inhibited approximately 80% of the labeled Fc binding. IgG antigen-antibody complexes inhibited 75% of the Fc binding. In the reciprocal experiment intact IgG and Fc inhibited binding of labeled IgG by 100%. The major cell population that bound IgG and Fc fragments in the spleen cell preparation was the B [bone marrow-derived] lymphocytes. Removal of macrophages did not significantly affect binding of labeled Fc fragments. T[thymus-derived]-cell-enriched populations bound an insignificant quantity of Fc fragments.