Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R

Cathepsin D from the muscle of bighead carp (Aristichthys no bilis, R.)was extracted ,purified and partially characterized . The extract ion and purification o f the enzyme was achieved byautolysis of the muscle,acetone precipitation, gelfiltrat ion on Sephadex G100-120 and on ionexchange carbox...

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主要作者: Bakar, Jamilah
格式: Thesis
語言:English
English
出版: 1993
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在線閱讀:http://psasir.upm.edu.my/id/eprint/8357/1/FSMB_1993_1_A.pdf
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總結:Cathepsin D from the muscle of bighead carp (Aristichthys no bilis, R.)was extracted ,purified and partially characterized . The extract ion and purification o f the enzyme was achieved byautolysis of the muscle,acetone precipitation, gelfiltrat ion on Sephadex G100-120 and on ionexchange carboxymethyl cellulose (CMC)column chromatography . It had a molecular weight(m.w)of 37,500-38,000 dalton (D) with a pH optimum at 3.2 and temperature optimum of 50°C. Myofibril was also optimally digested at pH3.2. The purified enzyme had a single major peptideband on sodiumdodecyl sulfate polyacrylamide gelelectrophoresis SDS-PAGE )and was completely inhibited by pepstatin .