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公猪精浆中17 kDa精子包被蛋白的纯化及部分特性分析

Purification and partial characterization of the 17 kDa sperm coating protein from boar seminal plasma.

作者信息

Moos J, Veselský L, Pĕknicová J, Drahorád J

机构信息

Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Prague.

出版信息

Mol Reprod Dev. 1992 Oct;33(2):165-71. doi: 10.1002/mrd.1080330208.

DOI:10.1002/mrd.1080330208
PMID:1418985
Abstract

Sperm coating proteins of 16, 17, and 19 kDa have been purified from boar seminal plasma. The 17 kDa protein has been identified as an antigen recognized by monoclonal antibody ACR.3 and is thus identical to low molecular mass zona pellucida binding protein from boar spermatozoa (Moos et al., 1990). The 17 and 19 kDa proteins are glycosylated and tend to form hetero-complexes. The 17 kDa ACR.3 antigen is sequentially released from the sperm cell surface during capacitation and, after induction of the acrosome reaction, the 16 kDa form was also observed. Immunocytochemical studies on boar reproductive tissues have suggested that the seminal vesicle epithelium may be the source of these proteins.

摘要

已从公猪精浆中纯化出了分子量为16、17和19千道尔顿的精子包被蛋白。17千道尔顿的蛋白已被鉴定为单克隆抗体ACR.3识别的一种抗原,因此与公猪精子的低分子量透明带结合蛋白相同(穆斯等人,1990年)。17和19千道尔顿的蛋白是糖基化的,并且倾向于形成异源复合物。在获能过程中,17千道尔顿的ACR.3抗原从精子细胞表面依次释放,并且在诱导顶体反应后,还观察到了16千道尔顿的形式。对公猪生殖组织的免疫细胞化学研究表明,精囊上皮可能是这些蛋白的来源。

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