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From the Department of Medicine, State University of New York at Buffalo, Buffalo, New York 14215
Abstract
IgG and IgM were isolated from 10 different species (human, monkey, horse, dog, cow, sheep, rabbit, chicken, rat and guinea pig) by a combination of starch block electrophoresis and Sephadex G-200 gel filtration. The patterns of heavy and light chains were studied in urea starch gel electrophoresis at pH 3.0 after reduction and alkylation. With the exception of the chicken 7S immunoglobulin, the electrophoretic patterns of IgG from the different species were remarkably similar. However, when IgM preparations from these species were compared, marked differences in mobility of the µ chains were seen. The immunologic cross-reactions of the IgG and IgM proteins from these same species were studied by quantitative complement fixation with three rabbit antisera specific for human 
chains and three specific for human µ chains. The nonprimate IgG cross-reacted weakly (5 to 30%) compared with nonprimate IgM preparations which cross-reacted strongly (30 to 55%). In accordance with the electrophoretic studies, the chicken 7S protein was uniquely different from the other IgG fractions and did not cross-react at all with various antihuman chain sera while chicken IgM showed good cross-reactivity.
Footnotes
1 This work was supported by National Institutes of Health Research Grants 2R01 AM-10419 to T. B. Tomasi, Jr. and AM-10428 to M. Reichlin. M. Reichlin is recipient of Research Career Development Award 5 K-03AM 20729.
2 Send reprint requests to: Dr. T. B. Tomasi, Jr., E. J. Meyer Memorial Hospital, Annex BB, 462 Grider Street, Buffalo, New York 14215.
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