Modifizierung von Argininresten in Pyruvat-Kinase
- 1 January 1977
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 358 (2) , 1565-1572
- https://doi.org/10.1515/bchm2.1977.358.2.1565
Abstract
Pyruvate kinase [EC 2.7.1.40] from pig heart is inactivated by the specific arginyl reagent phenylglyoxal. Loss of activity is caused by the reaction of a single molecule of phenylglyoxal per subunit of enzyme. During inactivation 3-6 arginyl residues are modified dependent on the concentration of phenylglyoxal used for modification. Solubility of the protein is reduced by modification. ATP or phosphoenolpyruvate protect against inactivation. A single arginine is less subject to chemical modification in their presence. An arginine may be essential at the substrate binding site. The activating ion K+ does not affect inactivation, whereas Mg2+ diminishes inactivation. Pyruvate kinase from rabbit muscle is modified by phenylglyoxal in a similar manner.This publication has 14 references indexed in Scilit:
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