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作 者:邱芳萍[1] 杜培革[2] 安丽萍[2] 吕刚[2] 李青山[3]
机构地区:[1]长春工业大学生物工程学院,长春130012 [2]北华大学医学院,吉林132000 [3]吉林大学生命科学学院,长春130021
出 处:《高等学校化学学报》2005年第6期1090-1092,共3页Chemical Journal of Chinese Universities
基 金:吉林省科学技术厅基础研究项目(批准号:2004128)资助.
摘 要: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.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.
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