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Acrosin‐Dependent Solubilization of Antigenic Peptides From Human Spermatozoa *
Author(s) -
CZUPPON A.B.,
METTLER L.
Publication year - 1981
Publication title -
american journal of reproductive immunology
Language(s) - English
Resource type - Journals
eISSN - 1600-0897
pISSN - 0271-7352
DOI - 10.1111/j.1600-0897.1981.tb00062.x
Subject(s) - acrosin , sperm , antiserum , peptide , antibody , chemistry , antigen , biochemistry , enzyme , sepharose , lysin , biology , microbiology and biotechnology , acrosome , immunology , escherichia coli , botany , bacteriophage , gene
Human spermatozoal polypeptides have been solubilized by incubation of spermatozoa in phosphate‐buffered saline. Inhibition of peptide release by the acrosin inhibitor N‐α‐tosyl‐L‐lysin‐chloromethyl suggests the direct involvement of the acrosomal enzyme in the liberation of the peptides. The peptides were coupled to activated Sepharose 4B gel and the peptide‐absorbed antibody of antispermatozoal antisera was detected with the aid of 125 I‐protein‐A tracer. The occurrence of three types of peptides became evident: one that binds to both sperm‐agglutinating and sperm‐immobilizing antibodies, one that binds to sperm‐immobilizing antibodies, and another that binds to sperm agglutinating antibodies only. The peptides might be of interest from an immunological point of view, because the relatively mild procedure of their solubilization could also prevail under physiological conditions, resulting in release of immunogenic peptides from spermatozoa in the genital tracts.