The use of absorption optics to measure dissociation of yeast enolase into enzymatically active monomers.
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Phosphoglycerate mutase is inactivated by butanedione in borate buffer. Inactivation by 0.13 mM reagent correlates with the modification of one arginyl residue per subunit, and is prevented by either 2, 3-diphosphoglycerate or 3-phosphoglycerate. With 0.50 mM butanedione, inactivation is accompanied by the modification of three arginyl residues per subunit, two of which are protected by the combined presence of cofactor and substrate.
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A precursor of the spore-lytic enzyme of Clostridium perfringens was extracted with alkali from dormant spores of the organism. The enzyme precursor was activated by incubating it with germinated spores which had been treated with alkali. The activation was greatly enhanced by the addition of 3-phosphoglycerate, suggesting that the conversion of precursor to active enzyme depends on endogenous energy-producing metabolism during germination.