SciELO - Scientific Electronic Library Online

vol.5 número1Efficient transformation of Penicillium chrysogenum mediated by Agrobacterium tumefaciens LBA4404 for cloning of Vitreoscilla hemoglobin geneApplication of rice (Oryza sativa L.) suspension culture in studying senescence in vitro (I).: Single strand preferring nuclease activity índice de autoresíndice de materiabúsqueda de artículos
Home Pagelista alfabética de revistas  

Servicios Personalizados




Links relacionados


Electronic Journal of Biotechnology

versión On-line ISSN 0717-3458


PETROVA, Ventsislava Yankova; RASHEVA, Tanya Vassileva  y  KUJUMDZIEVA, Anna V.. Catalase enzyme in mitochondria of Saccharomyces cerevisiae. Electron. J. Biotechnol. [online]. 2002, vol.5, n.1, pp.11-12. ISSN 0717-3458.

Catalase and superoxide dismutase activities have been explored in the yeast  Saccharomyces cerevisiae during batchwise growth experiment. During the diauxic growth in YPD medium high Ys values were obtained (0.415 - 0.423) and correlation between the total activities of both enzymes has been found. A mitochondrial fraction from three type strains of Saccharomyces cerevisiae has been isolated. The purity of this fraction was proved through different enzyme assays: hexokinase, glucose-6-phosphate dehydrogenase, D-amino acid oxidase, isocitric lyase, succinate dehydrogenase. Then the catalase, peroxidase, Mn and Cu/Zn superoxide dismutase activities were evaluated in the mitochondrial fraction. Polyacrylamide gel electrophoresis separations allowed to identify a mitochondrial catalase as a band of 0.239 Rm value. It differed from the two catalase specific bands with Rm values 0.218 and 0.257 obtained from the crude extract. It was proved that the three catalase proteins are charge isomers. A positive correlation between the activity of mitochondrial catalase and Mn superoxide dismutase also takes place. Molecular weight of mitochonrial catalase protein has been determined as 240 kD.

Palabras clave : .

        · texto en Inglés


Creative Commons License Todo el contenido de esta revista, excepto dónde está identificado, está bajo una Licencia Creative Commons