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PubMed · 32465

[Total activity of glucose oxidase, catalase and invertase and their distribution in the mycelial subcellular fractions of Penicillium vitale Pidopl. et Bilai].

E A Nikol'skaia·L M Kirillova·O I Siniavskaia
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CatalaseCell-Free SystemEnzyme ActivationGlucose OxidaseHydrogen-Ion ConcentrationPenicilliumSubcellular FractionsSucraseEnglish AbstractJournal Article

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E A Nikol'skaia, L M Kirillova, O I Siniavskaia. [Total activity of glucose oxidase, catalase and invertase and their distribution in the mycelial subcellular fractions of Penicillium vitale Pidopl. et Bilai].. https://pubmed.ncbi.nlm.nih.gov/32465/

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PubMed1979

The effects of platinum complexes on seven enzymes.

The effects of K2PtCl4, cis-Pt(NH3)2Cl2, and trans-Pt(NH3)2Cl2 on the activities of glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, dihydrofolate reductase, fructose-1,6-bisphosphate aldolase, catalase, tyrosinase, and peroxidase have been investigated. All of the enzymes which are thought to have essential sulfhydryl groups (glyceraldehyde-3-phosphate dehydrogenase, aldolase, and glucose-6-phosphate dehydrogenase) were significantly inhibited by K2PtCl4. The other four enzymes studied are not known to have essential sulfhydryl groups, and were not significantly affected by the Pt compounds under the conditions employed. Glyceraldehyde-3-phosphate dehydrogenase was the only enzyme inhibited by all three Pt compounds tested, with K2PtCl4 being the most effective and cis-Pt(NH3)2Cl2 the least effective inhibitor. Semilogarithmic plots of residual activity versus inhibition time indicated that the inhibition reactions were not simple first-order processes, except for the inhibition of glucose-6-phosphate dehydrogenase by K2PtCl4 which appeared to be first-order with respect to enzyme concentration.

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