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...
محفوظ في:
| المؤلف الرئيسي: | |
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| التنسيق: | أطروحة |
| اللغة: | English English |
| منشور في: |
1993
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| الموضوعات: | |
| الوصول للمادة أونلاين: | http://psasir.upm.edu.my/id/eprint/8357/1/FSMB_1993_1_A.pdf |
| الوسوم: |
إضافة وسم
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| الملخص: | 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 . |
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