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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1993
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my.upm.eprints.83572012-10-24T07:39:55Z http://psasir.upm.edu.my/id/eprint/8357/ Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R Bakar, Jamilah 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 . 1993 Thesis NonPeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/8357/1/FSMB_1993_1_A.pdf Bakar, Jamilah (1993) Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R. PhD thesis, Universiti Pertanian Malaysia. English |
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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 . |
format |
Thesis |
author |
Bakar, Jamilah |
spellingShingle |
Bakar, Jamilah Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R |
author_facet |
Bakar, Jamilah |
author_sort |
Bakar, Jamilah |
title |
Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R |
title_short |
Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R |
title_full |
Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R |
title_fullStr |
Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R |
title_full_unstemmed |
Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R |
title_sort |
effect of storage on the changes in cathepsin d activity, nucleotide contents, peptide profiles and muscle ultrastructure of aristichthys nobilis, r |
publishDate |
1993 |
url |
http://psasir.upm.edu.my/id/eprint/8357/1/FSMB_1993_1_A.pdf http://psasir.upm.edu.my/id/eprint/8357/ |
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1643823992918769664 |
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13.209306 |