Abstract
Abstract Rabbit secretory component (SC) of colostral secretory IgA (sIgA) was isolated following dissociation from the immunoglobulin in 5 M guanidine ·HC1. Two procedures were used, one yielding native SC and the other SC with all half-cystines carboxymethylated. The results of analytic and preparative zone electrophoresis in polyacrylamide gels led to a correlation between the antigenic activities used to define component polypeptide chains of sIgA and the characteristics of their electrophoretic mobility. The native form of a fast-migrating component (F-component) different from alpha, light and SC polypeptides was also isolated by preparative gel electrophoresis. Its cellular localization was compared with that of other components of sIgA.
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