A novel ubiquitin carboxyl terminal hydrolase is involved in toad oocyte maturation |
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Authors: | ZHAO GUI SUN WEI HUA KONG YAN JUN ZHANG SHAN YAN JI NING LU ZHENG GU FENG LIN JIA KE TSO |
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Institution: | National Laboratory of Contraceptives and Devices Research, Shanghai Institute of Planned Parenthood Research, Shanghai 200032, China;College of Life Science, Shandong University, Ji'nan 250100, China;Shandong University of Traditional Chinese Medicine, Ji'nan 250014,China College of Life Science, Shandong University, Ji'nan 250100, China College of Life Science, Shandong University, Ji'nan 250100, China National Laboratory of Contraceptives and Devices Research, Shanghai Institute of Planned Parenthood Research, Shanghai 200032, China National Laboratory of Contraceptives and Devices Research, Shanghai Institute of Planned Parenthood Research, Shanghai 200032, China National Laboratory of Contraceptives and Devices Research, Shanghai Institute of Planned Parenthood Research, Shanghai 200032, China National Laboratory of Contraceptives and Devices Research, Shanghai Institute of Planned Parenthood Research, Shanghai 200032, China National Laboratory of Contraceptives and Devices Research, Shanghai Institute of Planned Parenthood Research, Shanghai 200032, China |
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Abstract: | p28, a 28kD protein from toad (Bufo bufo gargarizans) oocytes, was identified by using p13suc1-agaroseaffinity chromatography. Sequence homology analysis of the full-length cDNA of p28 (Gene Bank accessionnumber: AF 314091) indicated that it encodes a protein containing 224 amino-acids with about 55% iden-tities and more than 70% positives to human, rat or mouse UCH-L1, and contains homological functionaldomains of UCH family. Anti-p28 monoclonal antibody, on injecting into the oocytes, could inhibit theprogesterone-induced resumption of meiotic division in a dose-dependent manner. The recombinant proteinp28 showed similar SDS/PAGE behaviors to the native one, and promoted ubiquitin ethyl ester hydrolysis,a classical catalytic reaction for ubiquitin carboxyl terminai hydrolases (UCHs). The results in this paperreveal that a novel protein, p28, exists in the toad oocytes, is a UCH L1 homolog, was engaged in theprocess of progesterone-induced oocyte maturation possibly through an involvement in protein turnover anddegradation. |
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Keywords: | p28 cDNA clone recombinant expression ubiquitin carboxyl terminal hydrolase oocyte maturation |
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