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生物学
Purification,Characterization and cDNA Cloning of a Myofibril-bound Serine Proteinase from the Skeletal Muscle of Crucian Carp(Carassius auratus)
<正>A myofibril-bound serine proteinase(MBSP)was highly purified from the skeletal muscle of crucian carp(carasius auratus)by acidic treatment of myofibril solution and chromatographies on Q-Sepharose and benzamidine-Sepharose 6B.MBSP revealed a main protein band of approximately 28 kDa on SDS-PAGE and was particularly inhibited by serine proteinase inhibitors.Substrate specificity analysis revealed that the enzyme specifically cleaved at the carboxyl side of arginine and lysine residues,suggesting the characteristic of a trypsin-type serine proteinase.MBSP gene was cloned based on the N-terminal sequence and the conserved active site peptide of serine proteinases together with 5'-RACE and 3'-RACE.The coding region gave an amino-acid sequence of 242 residues including the initiation methionine and a signal peptide of 20 residues.Amino acid residues of His~(60),Asp~(106)and Ser~(196)consisting the catalytic triad of serine proteinases were conserved in the sequence.Crucian carp MBSP shared relatively high identities with other serine proteinases,especially in well-conserved regions.
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中国食品科学技术学会第五届年会暨第四届东西方食品业高层论坛论文摘要集
2007年

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