Lactate dehydrogenase from cultured Aedes albopictus cells: kinetic and isozyme analysis.

Torres-da Matta, J; Silva, C B; Hassón-Voloch, A; Rebello, M A

Torres-da Matta, J; Silva, C B; Hassón-Voloch, A; Rebello, M A.

Afiliação

Torres-da Matta J; Laboratório de Físico-Química Biológica, Universidade Federal do Rio de Janeiro.

An Acad Bras Cienc ; 59(4): 433-7, 1987.

Article em En | MEDLINE | ID: mdl-3454571

RESUMO

L(+) lactate dehydrogenase (LDH) activity from cultured cells of Aedes albopictus was studied as a kinetic model of carbohydrate metabolism. Enzyme kinetics were studied in the forward (lactate as substrate) and reverse (pyruvate as substrate) reactions and the apparent Km values were obtained showing LDH higher affinity for pyruvate. The Hill coefficient values for each substrate were similar and indicate the existence of only one binding site on the enzyme. Isozyme analysis on cellulose-acetate electrophoresis presented a single band of LDH which presumably is of the LDH-5 type. The results obtained contribute to the assumption that Aedes albopictus cells have a predominance of anaerobic metabolism.

Assuntos

Aedes/enzimologia; L-Lactato Desidrogenase/metabolismo; Animais; Células Cultivadas; Isoenzimas; Cinética

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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aedes / L-Lactato Desidrogenase Limite: Animals Idioma: En Revista: An Acad Bras Cienc Ano de publicação: 1987 Tipo de documento: Article País de publicação: Brasil

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