4.6 Article

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

期刊

MOLECULAR HUMAN REPRODUCTION
卷 6, 期 5, 页码 429-434

出版社

OXFORD UNIV PRESS
DOI: 10.1093/molehr/6.5.429

关键词

epididymis; glycoprotein; human; sperm maturation

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据