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  • Title: Selective inhibition of an enzyme in crude cell extracts. The use of subunits modified with a half-of-the-sites reagent.
    Author: Muronetz VI, Ashmarina LI, Nagradova NK.
    Journal: Biochem Int; 1983 Apr; 6(4):443-50. PubMed ID: 6385975.
    Abstract:
    Yeast glyceraldehyde-3-phosphate dehydrogenase carboxymethylated at four active-site cysteine residues was incubated with a crude extract of baker's yeast. This resulted in a loss of the glyceraldehyde-3-phosphate dehydrogenase activity initially present in the extract. The extent of inactivation depended upon the ratio modified enzyme/enzyme present in the extract. Under appropriate conditions 63.1% inactivation of glyceraldehyde-3-phosphate dehydrogenase in crude extract could be achieved. The observed effect is explained in terms of hybridization between the carboxymethylated dimers of the purified enzyme and dimeric species of glyceraldehyde-3-phosphate dehydrogenase present in the crude extract, the inactivation being due to the influence of the half-of-the-sites reagent transmitted via the interdimeric contacts.
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