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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27041

Title: Epitope topology and removal of mouse acrosomal plasma membrane by P12-targeted immunoaggregation
Authors: Han-Jia Lin;Ching-Wei Luo;Chia-Yih Wang;Yee-Hsiung Chen
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Acrosomal removal;Epitope;Immunoagglutination;Protease inhibitor
Date: 2006-10-13
Issue Date: 2011-10-21T02:22:25Z
Publisher: Biochemical and Biophysical Research Communications
Abstract: Abstract:P12 is a Kazal-type trypsin inhibitor that has been purified from mouse seminal vesicle secretion. We observed a slight impact of P12 on sperm capacitation, and demonstrated the removal of plasma membrane overlaying the acrosome region by immunoaggregation of P12 on mouse sperm. Further, we compared the immunoreactivity of P12 antibody to ten P12 variants, including six single-site mutated mutants (R19L, Y21V, D22G, R43G, K44S, and R45T), two multisite mutated mutants (R43G/K44S/R45T and L50H/R52G/K53A), and two deletion mutants (Nd10 and Cd8) in which 10 and 8 residues were deleted from the N- and C-terminals, respectively. We found that the N-terminal region, 43RKR45, and the C-terminal region, but not R19, Y21, and D22, are involved in the three epitopes that reside on one side and are three-dimensionally distant from R19, Y21, and D22 on the P12 molecule. Based on the epitope topology, we elucidated the structural basis by which P12 antibody immunoaggregated P12 on sperm head.
Relation: 349(1), pp.284–288
URI: http://ntour.ntou.edu.tw/handle/987654321/27041
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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