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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my-upm-ir.83572012-10-24T07:39:55Z Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R 1993 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 . Bighead carp Animal extracts Peptides 1993 Thesis http://psasir.upm.edu.my/id/eprint/8357/ http://psasir.upm.edu.my/id/eprint/8357/1/FSMB_1993_1_A.pdf application/pdf en public phd doctoral Universiti Pertanian Malaysia Bighead carp Animal extracts Peptides Food Science and Technology English |
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Universiti Putra Malaysia |
collection |
PSAS Institutional Repository |
language |
English English |
topic |
Bighead carp Animal extracts Peptides |
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Bighead carp Animal extracts Peptides Bakar, Jamilah Effect of Storage on the Changes in Cathepsin D Activity, Nucleotide Contents, Peptide Profiles and Muscle Ultrastructure of Aristichthys Nobilis, R |
description |
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 |
qualification_name |
Doctor of Philosophy (PhD.) |
qualification_level |
Doctorate |
author |
Bakar, Jamilah |
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 |
granting_institution |
Universiti Pertanian Malaysia |
granting_department |
Food Science and Technology |
publishDate |
1993 |
url |
http://psasir.upm.edu.my/id/eprint/8357/1/FSMB_1993_1_A.pdf |
_version_ |
1747810787340058624 |