4.6 Article

Purification of GP-83, a glycoprotein secreted by the human epididymis and conjugated to mature spermatozoa

Journal

MOLECULAR HUMAN REPRODUCTION
Volume 6, Issue 5, Pages 429-434

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/molehr/6.5.429

Keywords

epididymis; glycoprotein; human; sperm maturation

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Epididymal secretions are critical for mammalian spermatozoa to acquire both forward motility and an ability to recognize and penetrate oocytes. Previous studies identified two glycoproteins, GP-83 and GP-39, which were secreted by the human epididymis and may be related to maturation of sperm function. In this study, GP-83 was purified from human seminal fluid by DEAE-ion exchange, gel filtration chromatography and preparative gel elution. The isoelectric point (pl) of purified GP-83 was 6.57, Monospecific antiserum to GP-83 was induced in male New Zealand rabbits and confirmed on immunoblots, GP-83 was found in fluid, tissue and sperm extracts of corpus and cauda epididymis, bur not in the caput. Immunohistochemical localization identified GP-83 in the luminal contents and in the supranuclear region and cell membrane of principal cells of the corpus and cauda epididymis. GP-83 was found on the anterior acrosome in ejaculated spermatozoa, and shifted to the equatorial region after capacitation and the acrosome reaction.

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