Purification of Epididymis-specific Protein from Porcine Seminal Plasmas and Its Primary Structure

Abstract

Abstract: Through successive chromatography on Q-sepharose, Matrex Red A, Superdex S-200 and Resource Q chromatography column, epididymis-specific protein from porcine seminal plasma was purified. Epididymis-specific protein(PE4) was purified to homogeneity by polyacrylamide gel electrophoresis. The molecular weight of the purified protein was calculated to be about 11 000 on SDS-PAGE. The whole primary structure of the purified epididymis-specific protein was determined by N-terminal amino acid sequence analysis, digestion of lysyl-endo-peptidase and BrCN. The primary structure of PE4 showed a significant similarity to those of epididymis-specific protein-4(HE4). The level of amino acid homology was 78.49%. Then, it indicates that epididymis-specific protein belonged to disulfide-core-protein of antileukocyte proteinase inhibitor(ALP) and there is a important function in sperm maturation.

Key words: Porcine, Epididymis, Specific protein, Purification, Primary structure

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QIU Fang-Ping, DU Pei-Ge, AN Li-Ping, LV Gang, LI Qing-Shan . Purification of Epididymis-specific Protein from Porcine Seminal Plasmas and Its Primary Structure[J]. Chem. J. Chinese Universities, 2005, 26(6): 1090.

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Purification of Epididymis-specific Protein from Porcine Seminal Plasmas and Its Primary Structure

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