The effect of ions and adenosine nucleotides on the activity of lactate dehydrogenase from the epaxial muscle of fish
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Data
1996-12-01
Autores
Ocampos, Dario
Rosa, Rubens
Rodrigues, Edson
Da Silva Gilli, Marcia Monteiro
Rosa, Claudete Deguirmendjian [UNESP]
Bacila, Metry
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Lactate dehydrogenase was partially purified from the epaxial muscle of Piaractus mesopotamicus (pacu) and its hybrid Piaractus mesopotamicus x Colossoma macropomus (tambacu). This preparation was used for kinetic studies carried out at pH 6.0 and 7.5. It was also used for the study of the inhibition properties of adenosine nucleotides = ATP, ADP, AMP =, divalent ions Ni2+, Cu2+, Co2+ and the anions oxamate and oxalate.
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Arquivos de Biologia e Technologia, v. 39, n. 2, p. 463-470, 1996.