Biochemical studies in marine species - II. NADP+-dependent isocitrate dehydrogenase from turbot (Scophthalmus maximum L.) larvae
8 páginas, 4 tablas, 7 figuras The isocitrate dehydrogenase activity specific for NADP + has been studied in early turbot larvae and compared with that of their adult counterparts. The activity showed a broad optimum pH between 7.9 and 9.0, and an optimum temperature of 400C (with an E, of 23.3 k J/...
| Published in: | Comparative Biochemistry and Physiology Part B: Comparative Biochemistry |
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| Main Author: | |
| Format: | Article in Journal/Newspaper |
| Language: | English |
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Elsevier
1994
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| Subjects: | |
| Online Access: | http://hdl.handle.net/10261/60075 https://doi.org/10.1016/0305-0491(94)90225-9 |
| Summary: | 8 páginas, 4 tablas, 7 figuras The isocitrate dehydrogenase activity specific for NADP + has been studied in early turbot larvae and compared with that of their adult counterparts. The activity showed a broad optimum pH between 7.9 and 9.0, and an optimum temperature of 400C (with an E, of 23.3 k J/tool) and was inhibited by high ionic strength and heavy metals. The apparent K, values for the substrates were 16.7 pM for isocitrate, 3.5 for NADP +, 29.6 pM for Mk~ + and 3.3/JM for the Mg-isocitrate complex. The effect of the absence of Mk~ + on the enzyme affinity for its substrates is also reported. The enzyme stability was decreased by iodoacetic acid and this effect reverted by isocitrate. The enzyme activity was inhibited by metabolites such as citrate, oxoglutarate and adenine dinucleotides. It was also fully inhibited by the concerted action of glyoxylate and oxaloacetate. This work has been supported by a grant from the Xunta de Galicia No. XUGA40201B90. Peer reviewed |
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