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Specific binding of the glycosaminoglycan /sup 3/H-heparin to bull, monkey, and rabbit spermatozoa in vitro

Journal Article · · J. Androl.; (United States)
OSTI ID:6983241
In Vitro binding and some binding parameters of the glycosaminoglycan heparin to viable epididymal or ejaculated bull spermatozoa, ejaculated rabbit spermatozoa, and frozen-thawed rhesus monkey spermatozoa were investigated. Nonspecific binding was affected only by the concentration of /sup 3/H-heparin, whereas specific binding was saturable, reversible, and dependent on the pH, temperature, and calcium concentration of the incubation medium. Magnesium concentration dependence was observed in the presence of calcium but could not be detected in the absence of calcium. Bound /sup 3/H-heparin was displaced by several orders of magnitude greater concentrations of chondroitin sulfate. Scatchard plot analysis suggested multiple binding affinities for /sup 3/H-heparin to spermatozoa. /sup 3/H-heparin was shown to bind to sperm heads and flagella. Fluorescein-labeled heparin bound to acrosomal, postacrosomal, and flagellar membranes. It was concluded that the specific binding of heparin involved a proteinaceous component on, or intercalated with, spermatozoal membranes. Thus, glycosaminoglycans present in the female reproductive tract may contribute to sperm capacitation and enhance the likelihood of successful fertilization in mammals.
Research Organization:
Department of Dairy Science, University of Wisconsin, Madison
OSTI ID:
6983241
Journal Information:
J. Androl.; (United States), Journal Name: J. Androl.; (United States) Vol. 5:2; ISSN JOAND
Country of Publication:
United States
Language:
English