The evidence of gene duplication for S-form NADP-linked isocitrate dehydrogenase in carp and goldfish

Quiroz-Gutierrez, Antonio; Ohno, Susumu

doi:10.1007/bf00484021

Cited by 27 publications

(2 citation statements)

References 13 publications

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“…Recently the supernatant NADP-isocitrate dehydrogenase has also been reported to occur in isoenzymic forms in bacteria (Reeves, Brehmeyer & Ajl, 1968;Self & Weitzman, 1970), in the carp and in the trout, both of which are thought to be tetraploid (Quiroz. Gutierrez & Ohno, 1970;Wolf, Engel & Faust, 1970).…”

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Temperature and enzyme activity in poikilotherms. Isocitrate dehydrogenases in rainbow-trout liver

Moon

Hochachka

1971

Biochemical Journal

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1. The kinetics of the thermally induced enzyme variants of the supernatant NADP-isocitrate dehydrogenase from rainbow-trout liver are investigated. 2. Fish acclimatized to 2 degrees C (cold-adapted enzyme) and 17 degrees C (warm-adapted enzyme) show different relative distributions of the three NADP-isocitrate dehydrogenase isoenzymes; this has been demonstrated with electrophoresis and electrofocusing techniques. 3. Plots of K(m) versus temperature for the cold-adapted and warm-adapted enzyme variants are complex in nature with apparent maximal enzyme-substrate affinity corresponding to the temperature at which the trout is acclimatized. Both substrates, dl-isocitrate and NADP(+), give similar curves although the magnitude of the K(m) change with temperature is much decreased in the case of NADP(+). 4. E(a) values of approx. 18kcal/mol were determined for both the cold-adapted and warm-adapted enzyme variants. 5. In an attempt to determine how velocities can be increased at low temperatures, cation, pH requirements, metabolite and enzyme concentrations were examined. 6. NAD-isocitrate dehydrogenase could not be detected in trout tissues.

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Temperature and enzyme activity in poikilotherms. Isocitrate dehydrogenases in rainbow-trout liver

Moon

Hochachka

1971

Biochemical Journal

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“…Quiroz-Gutierrez & Ohno (1970) have shown for a number of fish species that the heart form of NADP-isocitrate dehydrogenase is located specifically in mitochondria while the liver form is cytoplasmic. Electrophoresis of heart extracts of Atlantic salmon yields a single, invariant band while three phenotypes were observed in liver extracts (Plate I).…”

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confidence: 99%

NADP‐isocitrate dehydrogenase polymorphism in the Atlantic salmon Salmo salar

Cross¹,

Payne²

1977

Journal of Fish Biology

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Electrophoretic variation of Atlantic salmon NADP-isocitrate dehydrogenase in liver extracts of material from Ireland is interpreted in terms of two loci, IDH-A and IDH-B, coding for cytoplasmically-located isozymes. The IDH-A locus is polymorphic with q1DH-A1=0.18 and qIDH-AZ=0*82. This polymorphism is of potential value for investigating the population genetics of the two races of Atlantic salmon in Ireland. An additional, monomorphic band which appears in heart extracts may be a mitochondria1 enzyme coded by a third locus.

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Isocitrate dehydrogenases from liver ofSqualus acanthias (spiny dogfish) and citrate formation by isolated mitochondria

1996

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The evidence of gene duplication for S-form NADP-linked isocitrate dehydrogenase in carp and goldfish

Cited by 27 publications

References 13 publications

Temperature and enzyme activity in poikilotherms. Isocitrate dehydrogenases in rainbow-trout liver

Temperature and enzyme activity in poikilotherms. Isocitrate dehydrogenases in rainbow-trout liver

NADP‐isocitrate dehydrogenase polymorphism in the Atlantic salmon Salmo salar

Isocitrate dehydrogenases from liver ofSqualus acanthias (spiny dogfish) and citrate formation by isolated mitochondria

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