摘要：Después de crecer células de la cepa YR-1 de Mucor circinelloides en naftaleno como única fuente de carbono, fue revelada la presencia de cinco actividades: 1, 2-dihidroxi-1, 2-dihidro-naftalendiol deshidrogenasa mediante zimogramas electroforéticos, utilizando (+)-cis- 1(R), 2(s)-dihidroxi-1, 2-dihidronaftaleno como sustrato y NADP+ como aceptor de electrones. Las bandas NDD1, NDD3 y NDD5 que mostraron una mayor intensidad en los zimogramas y por su movilidad electroforética, fueron purificadas a homogeneidad por pasos secuenciales de electroforesis-electroelución para conocer tanto el peso molecular, como el número de subunidades que conforman a cada banda de actividad. Los resultados mostraron pesos moleculares de 98.64 kDa, 48.87 kDa y 102.45 kDa, para cada subunidad respectiva. Se concluye que las actividades no son isoformas conformadas por la misma subunidad proteica, las enzimas nativas son homopoliméricas y no contienen subunidades protoméricas compartidas.
其他摘要：After the growth of cells of strain YR-1 of Mucor circinelloides with naphthalene as sole carbon source, the presence of five different 1, 2-dihydroxi-1, 2-dihydro-naphthalenediol dehydrogenase activities were revealed by electrophoretic zymograms using (+)-cis-1(R), 2(s)-dihydroxi-1, 2-dihydronaphthalene as substrate and NADP+ as electron acceptor. The bands NDD1, NDD3 and NDD5 showing the highest intensity in the zymograms and by their relative electrophoretic mobilities, were purified to homogeneity by means of sequential steps of electrophoresis-electroelution to know both, the molecular weight and the number of subunits that conform each activity band. The results show molecular weights of 98.64 kDa, 48.37 kDa and 102.45 kDa for the subunit of each protein band respectively. We conclude that these activities there are not enzymatic isoforms conformed by the same proteic subunit, the native enzymes have a homopolymeric structure and they do not share any protomeric subunit.
