title: Bifunctionality and pseudoisozymes of pyruvate kinase from codfish muscle.
abstract: Pyruvate kinase has been purified from codfish muscle. The ratio of phosphotransferase and oxalacetate decarboxylase activities remains relatively constant throughout purification steps. These two activities are dependent as well as sensitive to sulfhydryl reagents. In the presence of dithioerythritol, only one molecular form of pyruvate kinase is detected. However, the enzyme exists as four pseudoisozymes in the presence of 2-mercaptoethanol. The pseudoisozymes of codfish pyruvate kinase are interconvertible under the influence of sulfhydryl reagents.
mesh_terms: D000818:Animals; D002262:Carboxy-Lyases / Q000378:metabolism; D004226:Dithioerythritol / Q000494:pharmacology; D005399:Fishes / Q000378:metabolism*; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008623:Mercaptoethanol / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology*; D010770:Phosphotransferases / Q000378:metabolism; D011770:Pyruvate Kinase / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D007527:Isoenzymes; D008623:Mercaptoethanol; D004226:Dithioerythritol; D010770:Phosphotransferases; D011770:Pyruvate Kinase; D002262:Carboxy-Lyases; C021916:oxaloacetate decarboxylase