Some aspects of isozymes of lactate dehydrogenase, malate dehydrogenase and glucosephosphate isomerase in fish

Basaglia, Fulvia

doi:10.1016/0305-0491(89)90269-1

Cited by 22 publications

(22 citation statements)

References 79 publications

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“…Almost every bony fish has the LDH-C* locus, which is believed to have originated through a duplication of the LDH-B* locus (Basaglia, 1989;Rao et. al., 1989).…”

Section: Discussionmentioning

confidence: 99%

“…The LDH-C* locus in bony fish shows different tissue regulation patterns in different taxons. Primitive orders of bony fish have a generalized tissue expression, while representatives of more advanced orders show a specialized tissue pattern (Whitt, 1975;Kettler and Whitt, 1986;Basaglia, 1989;Rao et al 1989). LDH-C* locus activity was not detected in the tissues (liver, muscle, heart and eye) analyzed for the lactate dehydrogenase system.…”

Section: Discussionmentioning

confidence: 99%

“…Panepucci et al (l984 and l987), Basaglia (1989), Rao et al (1989), Renno et al (1989), Degani and Veith (1990), , Verneau et al (1994), Zawadzki (1996), Revaldaves et al (l997) and Almeida and Sodré (l998), among many others.…”

Section: Introductionmentioning

confidence: 97%

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Genetic variability in five species of Anostomidae (Ostariophysi - Characiformes)

Chiari

Sodré

1999

Genet. Mol. Biol.

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Genetic variability was studied in five fish species (Anostomidae): Schizodon intermedius and S. nasutus and Leporinus friderici, L. elongatus and L. obtusidens, collected at one location on the Tibagi River (Paraná, Brazil). The protein data from seven systems coded collectively for 19 loci in the liver, muscle and heart. Nine of these loci were polymorphic. The estimated proportion of polymorphism loci (P) varied from 16.7% in S. intermedius to 36.9% in L. friderici; the mean heterozygosity observed (Ho) was 0.027 ± 0.015 and 0.109 ± 0.042, respectively. The estimated value of the genetic identity among L. friderici and S. intermedius (0.749) and S. nasutus (0.787) suggested that these are "congeneric" species. Morphological characteristics indicate that these species belong to distinct genera, while isoenzymatic data show that they are very similar at the genetic/biochemical level.

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“…Almost every bony fish has the LDH-C* locus, which is believed to have originated through a duplication of the LDH-B* locus (Basaglia, 1989;Rao et. al., 1989).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Genetic variability in five species of Anostomidae (Ostariophysi - Characiformes)

Chiari

Sodré

1999

Genet. Mol. Biol.

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“…LDH-4 and LDH-5 which contain mainly M subunits permit rapid accumulation of lactate, and are found in skeletal muscle where anaerobic glycolysis predominates, whereas LDH-1 and LDH-2 containing mainly H subunits are found in heart, where pyruvate is oxidized via the Krebs cycle (Basaglia, 1989). Very little information is available on LDH from reptiles.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of lactate dehydrogenase from Varanus liver

Javed

Azimuddin²,

Hussain³

et al. 1997

Exp Mol Med

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Lactate dehydrogenase was purified 21-fold from liver of Varanus bengalensis using colchicinesepharose column chromatography. The crude enzyme showed two isoenzymes (LDH-5 and LDH-4 ) by agarose gel electrophoresis (AGE). The p u r i f i e d enzyme showed a single band after SDS-PAGE corresponding to molecular mass of 35 kDa. The molecular mass of native enzyme was about 140 kDa. The optimum pH for the forward reaction was 7.5 while that for the reverse reaction was pH 9.5. The K m values for pyruvate, NADH, lactate and NAD + were 0.17 ± 0.037, 0.02 ± 0.004, 12.4 ± 3.05 and 0.38 ± 0.032 mM, respectively. Pre-heating of enzyme showed that its t 5 0 was 40-50˚C. Oxalate and n-hexanediol were inhibitors for both forward and reverse reactions. Among divalent ions, Cu + + was shown to be more effective inhibitor for the forward reaction. K e y w o r d s : LDH isoenzyme,

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“…The large increase in MDH activity in white muscle from 1 l~ grass carp is most likely due to a large increase in the thermolabile cMDH, but a smaller increase of the thermostable cMDH. The thermolabile form was more dominant only in muscle tissues for most fishes, while the thermostable form was present in greater quantities in all tissues (Basaglia 1989;Coppes 1990). Moreover, during low-temperature acclimation, !ipogensis is favored over gluconeogensis (Lin 1993;Woo 1990), but the latter is the most dominant pathway in liver.…”

Section: Discussionmentioning

confidence: 99%

Qualitative and quantitative strategies of thermal adaptation of grass carp (Ctenopharyngodon idella) cytoplasmic malate dehydrogenases

Lin

MacLeod

Kuo

1996

Fish Physiol Biochem

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Malate dehydrogenase isozymes of grass carp,Ctenopharyngodon idella, were identified by mitochondrial preparation and thermal denaturation. The structural and kinetic characteristics of chromatographically separated thermostable and thermolabile cMDHs were different in (1) half-life at 42°C, 10 min and 24 h, respectively, (2) optimal substrate, oxaloacetate and malate, concentrations, and (3) the apparent Michaelis-Menten constants of NADH and oxaloacetate.Total MDH activity in white muscle of 11°C-acclimated fish was about twice that of the 30°C-acclimated group. In addition, the ratio of the thermostable to thermolabile cMDH activity in white muscle of 30°C-acclimated fish was significantly higher than that of 11°C-acclimated fish. These results suggest that temperature acclimation can induce temperature compensation in MDH activity and differential expression of thermostable and thermolabile cMDH isozymes in freshwater fish.

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Some aspects of isozymes of lactate dehydrogenase, malate dehydrogenase and glucosephosphate isomerase in fish

Cited by 22 publications

References 79 publications

Genetic variability in five species of Anostomidae (Ostariophysi - Characiformes)

Genetic variability in five species of Anostomidae (Ostariophysi - Characiformes)

Purification and characterization of lactate dehydrogenase from Varanus liver

Qualitative and quantitative strategies of thermal adaptation of grass carp (Ctenopharyngodon idella) cytoplasmic malate dehydrogenases

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