Cloning of beta-microseminoprotein of the rat: A rapidly evolving mucosal surface protein

被引:37
作者
Fernlund, P
Granberg, L
Larsson, I
机构
[1] Department of Clinical Chemistry, University of Lund, Malmö General Hospital
关键词
amino acid sequencing; disulfide bonds; molecular evolution; mucus; prostate; protein; seminal plasma; western blot;
D O I
10.1006/abbi.1996.0431
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
beta-Microseminoprotein is a small, nonglycosylated protein, rich in disulfide bonds, which is present in the secretions of the airways, the gastrointestinal tract, and the urogenital tract. Its function is unknown. It was originally characterized in the human and it has been difficult to identify the homologous protein in species other than primates. We have purified beta-microseminoprotein from rat prostate and from amino acid sequencing we have been able to clone the protein. The results reinforce conclusions reached earlier that beta-microseminoprotein is a rapidly evolving protein. Overall amino acid identities are only 45, 50, and 40% when the rat protein is compared with the proteins from the human, the ape, and the pig, respectively. However, the 10 cysteines are all completely invariant between these four species. The cloning of beta-microseminoprotein in the rat have substantially improved the possibilities to reveal the function of this mucosal surface protein. (C) 1996 Academic Press, Inc.
引用
收藏
页码:73 / 82
页数:10
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