LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae)
1. 1. LDH of Mylossoma duriventris and Colossoma macropomum examined by reduction of pyruvate, showed inhibition by low pH (pH 6.0) and activation by high pH (pH 8.5). The optimal pH in this direction was obtained at pH 8.5 and in reverse direction (oxidation of lactate), between pH 9.0 and 10.0. Th...
| Autor principal: | Almeida-Val, Vera Maria Fonseca |
|---|---|
| Outros Autores: | Schwantes, Maria Luíza Barcellos, Val, Adalberto Luis |
| Grau: | Artigo |
| Idioma: | English |
| Publicado em: |
Comparative Biochemistry and Physiology -- Part B: Biochemistry and
2020
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| Assuntos: | |
| Acesso em linha: |
https://repositorio.inpa.gov.br/handle/1/19540 |
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oai:repositorio:1-19540 |
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oai:repositorio:1-19540 LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae) Almeida-Val, Vera Maria Fonseca Schwantes, Maria Luíza Barcellos Val, Adalberto Luis Isoenzyme Lactate Dehydrogenase Pyruvic Acid Animals Tissue Fish Heart Muscle Nonhuman Priority Journal Temperature Animalsia Colossoma Macropomum Mylossoma Serrasalmidae Vertebrata 1. 1. LDH of Mylossoma duriventris and Colossoma macropomum examined by reduction of pyruvate, showed inhibition by low pH (pH 6.0) and activation by high pH (pH 8.5). The optimal pH in this direction was obtained at pH 8.5 and in reverse direction (oxidation of lactate), between pH 9.0 and 10.0. The effect of pH was temperature dependent. 2. 2. The activity of M. duriventris lactate dehydrogenase was increased by high temperatures while the C. macropomum LDH, unlike most vertebrates, was independent of the assay temperature. Also the Km (pyr) values proved to be temperature insensitive in heart muscle LDH from C. macropomun (pH 6.0 and 7.5). 3. 3. Some kinetic parameters, particularly the pyruvate inhibition, expressed as L/H ratios, showed a low divergence between the paralogous LDH loci in both species. 4. 4. The main differences between orthologous isozymes seems to rely on Ldh-B products. This fact corroborates the differences obtained in electrophoretic patterns. © 1991. 2020-06-15T22:09:42Z 2020-06-15T22:09:42Z 1991 Artigo https://repositorio.inpa.gov.br/handle/1/19540 10.1016/0305-0491(91)90311-Z en Volume 98, Número 1, Pags. 79-86 Restrito Comparative Biochemistry and Physiology -- Part B: Biochemistry and |
| institution |
Instituto Nacional de Pesquisas da Amazônia - Repositório Institucional |
| collection |
INPA-RI |
| language |
English |
| topic |
Isoenzyme Lactate Dehydrogenase Pyruvic Acid Animals Tissue Fish Heart Muscle Nonhuman Priority Journal Temperature Animalsia Colossoma Macropomum Mylossoma Serrasalmidae Vertebrata |
| spellingShingle |
Isoenzyme Lactate Dehydrogenase Pyruvic Acid Animals Tissue Fish Heart Muscle Nonhuman Priority Journal Temperature Animalsia Colossoma Macropomum Mylossoma Serrasalmidae Vertebrata Almeida-Val, Vera Maria Fonseca LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae) |
| topic_facet |
Isoenzyme Lactate Dehydrogenase Pyruvic Acid Animals Tissue Fish Heart Muscle Nonhuman Priority Journal Temperature Animalsia Colossoma Macropomum Mylossoma Serrasalmidae Vertebrata |
| description |
1. 1. LDH of Mylossoma duriventris and Colossoma macropomum examined by reduction of pyruvate, showed inhibition by low pH (pH 6.0) and activation by high pH (pH 8.5). The optimal pH in this direction was obtained at pH 8.5 and in reverse direction (oxidation of lactate), between pH 9.0 and 10.0. The effect of pH was temperature dependent. 2. 2. The activity of M. duriventris lactate dehydrogenase was increased by high temperatures while the C. macropomum LDH, unlike most vertebrates, was independent of the assay temperature. Also the Km (pyr) values proved to be temperature insensitive in heart muscle LDH from C. macropomun (pH 6.0 and 7.5). 3. 3. Some kinetic parameters, particularly the pyruvate inhibition, expressed as L/H ratios, showed a low divergence between the paralogous LDH loci in both species. 4. 4. The main differences between orthologous isozymes seems to rely on Ldh-B products. This fact corroborates the differences obtained in electrophoretic patterns. © 1991. |
| format |
Artigo |
| author |
Almeida-Val, Vera Maria Fonseca |
| author2 |
Schwantes, Maria Luíza Barcellos Val, Adalberto Luis |
| author2Str |
Schwantes, Maria Luíza Barcellos Val, Adalberto Luis |
| title |
LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae) |
| title_short |
LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae) |
| title_full |
LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae) |
| title_fullStr |
LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae) |
| title_full_unstemmed |
LDH isozymes in amazon fish-II. Temperature and pH effects on LDH kinetic properties from Mylossoma duriventris and Colossoma macropomum (Serrasalmidae) |
| title_sort |
ldh isozymes in amazon fish-ii. temperature and ph effects on ldh kinetic properties from mylossoma duriventris and colossoma macropomum (serrasalmidae) |
| publisher |
Comparative Biochemistry and Physiology -- Part B: Biochemistry and |
| publishDate |
2020 |
| url |
https://repositorio.inpa.gov.br/handle/1/19540 |
| _version_ |
1787142615994466304 |
| score |
11.755432 |