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| 12. |  | PANEPUCCI, L.; SCHWANTES, M. L.; SCHWANTES, A. R. Biochemical and physiological properties of the lactate Dehydrogenase allozymes of the Brazilian teleost, Leporinus friderici, anostomidae, cypriniformes. Comp. Biochem. Physiol., v.87B, n.1, p.199-206, 1987.| Biblioteca(s): Embrapa Pecuária Sudeste. |
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| Registros recuperados : 24 | |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Pecuária Sudeste. Para informações adicionais entre em contato com cppse.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Pecuária Sudeste. |
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Data corrente: |
04/12/1996 |
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Data da última atualização: |
23/06/2021 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
Nacional - B |
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Autoria: |
PANEPUCCI, L.; SCHWANTES, M. L.; SCHWANTES, A. R. |
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Afiliação: |
LUCIA PANEPUCCI, EMBRAPA-UEPAE de São Carlos, São Carlos, SP.; M. L. SCHWANTES, UFSCAR; A. R. SCHWANTES, UFSCAR. |
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Título: |
Biochemical and physiological properties of the lactate Dehydrogenase allozymes of the Brazilian teleost, Leporinus friderici, anostomidae, cypriniformes. |
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Ano de publicação: |
1987 |
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Fonte/Imprenta: |
Comp. Biochem. Physiol., v.87B, n.1, p.199-206, 1987. |
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Idioma: |
Inglês |
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Conteúdo: |
-l. Lactate dehydrogenase polymorphism of Leporinusfriderici is determined by two loci, each one encoded by two alleles--Ldh-A, Ldh-A' and Ldh-B and Ldh-B'. 2. Biochemical characterization of the different LDH phenotypes was carded out. Substrate saturation curves show that extracts, where the LDH-B predominates, are much more sensitive to substrate inhibition and have higher thermostability than skeletal muscle extracts where the LDH-A predominates. 3. Pyruvate affinity parameters of the different LDH-B phenotypes show differential values in all temperatures assayed. LDH-BB phenotypes presented always greater affinity values than the LDH-BB' and B'B' ones. 4. The different LDH-B phenotypes show differential thermostability when tested at 65°C, so, the LDH-B'B' phenotype had higher stability than the LDH-BB' and LDH-BB phenotypes. This was corroborated with the isozymes partially purified. 5. A variation was detected in the LDH-B phenotype frequencies since the experiment was started in 1980. 6. All these features suggest that this polymorphism may have an adaptive significance in relation to environmental variability, i.e. temperature fluctuations and water pollution due to industrial waste that notably increased in these last years. |
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Palavras-Chave: |
Biochemical; Physiological properties; Propriedade fisiológicas. |
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Thesagro: |
Bioquímica. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 01914naa a2200193 a 4500
001 1043348
005 2021-06-23
008 1987 bl uuuu u00u1 u #d
100 1 $aPANEPUCCI, L.
245 $aBiochemical and physiological properties of the lactate Dehydrogenase allozymes of the Brazilian teleost, Leporinus friderici, anostomidae, cypriniformes.$h[electronic resource]
260 $c1987
520 $a-l. Lactate dehydrogenase polymorphism of Leporinusfriderici is determined by two loci, each one encoded by two alleles--Ldh-A, Ldh-A' and Ldh-B and Ldh-B'. 2. Biochemical characterization of the different LDH phenotypes was carded out. Substrate saturation curves show that extracts, where the LDH-B predominates, are much more sensitive to substrate inhibition and have higher thermostability than skeletal muscle extracts where the LDH-A predominates. 3. Pyruvate affinity parameters of the different LDH-B phenotypes show differential values in all temperatures assayed. LDH-BB phenotypes presented always greater affinity values than the LDH-BB' and B'B' ones. 4. The different LDH-B phenotypes show differential thermostability when tested at 65°C, so, the LDH-B'B' phenotype had higher stability than the LDH-BB' and LDH-BB phenotypes. This was corroborated with the isozymes partially purified. 5. A variation was detected in the LDH-B phenotype frequencies since the experiment was started in 1980. 6. All these features suggest that this polymorphism may have an adaptive significance in relation to environmental variability, i.e. temperature fluctuations and water pollution due to industrial waste that notably increased in these last years.
650 $aBioquímica
653 $aBiochemical
653 $aPhysiological properties
653 $aPropriedade fisiológicas
700 1 $aSCHWANTES, M. L.
700 1 $aSCHWANTES, A. R.
773 $tComp. Biochem. Physiol.$gv.87B, n.1, p.199-206, 1987.
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