Studies on aminotransferase enzymes in fish and shellfish
The distribution of aspartate aminotransferase (AAT) and alanine aminotransferase (ALAT) activities in the skeletal muscle of several fish species is reported. AAT activity is found higher than ALAT activity and that the red muscle has higher aminotransferase activity than the white muscle. It is observed that 2-oxoglutaric acid has a wider scope as an amino group acceptor than pyruvic acid in the skeletal muscle of fish. The significance of transamination& in fish is discussed.
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| Main Authors: | , |
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| Format: | article biblioteca |
| Language: | English |
| Published: |
1980
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| Subjects: | Chemistry, aspartate aminotransferase, alanine aminotransferase, enzymes, biological transamination, Megalaspis cordyla, Rastrelliger kanagurta, Scomberomorus guttatus, Pampus argenteus, Otolithus argenteus, Psettodes erumei, Trichiurus savala, Trachysurus dussumieri, Harpodon nehereus, Scoliodon sorrakowah, Cyprinus carpio, Penaeus monodon, |
| Online Access: | http://hdl.handle.net/1834/33504 |
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| Summary: | The distribution of aspartate aminotransferase (AAT) and alanine aminotransferase (ALAT) activities in the skeletal muscle of several fish species is reported. AAT activity is found higher than ALAT activity and that the red muscle has higher aminotransferase activity than the white muscle. It is observed that 2-oxoglutaric acid has a wider scope as an amino group acceptor than pyruvic acid in the skeletal muscle of fish. The significance of transamination& in fish is discussed. |
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