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Zinc binding to major human seminal coagulum proteins
G Frenette1, R R Tremblay, J Y Dubé
1Laboratory of Hormonal Bioregulation, Laval University Hospital Centre, Ste-Foy, Québec, Canada.
Archives of Andrology
|January 1, 1989
Summary
This study found that human ejaculate proteins bind significant amounts of zinc, particularly in seminal plasma. Zinc binding to proteins decreases rapidly during sperm liquefaction, but its role remains unclear.
Area of Science:
- Biochemistry
- Reproductive Biology
- Urology
Background:
- Zinc is a vital trace element with crucial roles in male reproductive physiology.
- Understanding zinc's interaction with seminal plasma proteins is key to reproductive health.
Purpose of the Study:
- To investigate the in vitro binding of zinc to proteins in human ejaculate and male accessory gland secretions.
- To explore the relationship between zinc binding, seminal plasma coagulation, and liquefaction.
Main Methods:
- Proteins were separated using sodium dodecyl sulfate gel electrophoresis and transferred to nitrocellulose filters.
- Filters were incubated with 65ZnCl2 to assess zinc binding.
- Zinc concentrations were measured in different seminal fractions.
Main Results:
- High zinc binding was observed in approximately 20 protein bands (14-70 kDa) of coagulated seminal plasma.
- Zinc binding decreased rapidly with sperm liquefaction, primarily affecting high-molecular-weight proteins.
- Low zinc binding occurred in spermatozoa, with virtually none in epididymal and prostatic fluids.
Conclusions:
- Seminal vesicle proteins are the primary extracellular targets for prostatic zinc in humans.
- The precise role of zinc binding in seminal coagulation and liquefaction remains undetermined.
- Further research is needed to elucidate the functional significance of zinc-protein interactions in human semen.