Correlations between enzymes of energy-supplying metabolism as a basic pattern of organization in muscle

• Published in: Comparative biochemistry and physiology. B, Comparative biochemistry Vol. 41; no. 3; pp. 533 - 540
• Main Authors: Staudte, H.W., Pette, D.
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 15.03.1972
• Subjects: 3-hydroxyacyl-CoA dehydrogenase; Adenosine Monophosphate; adenylate kinase; Alcohol Oxidoreductases - analysis; Animals; Birds; citrate synthase; Citrates; Coenzyme A; comparative enzymology; constant-proportion enzyme groups and metabolic correlations; creatine kinase; Creatine Kinase - analysis; energy-supplying metabolism; Glyceraldehyde-3-Phosphate Dehydrogenases - analysis; Glycerolphosphate Dehydrogenase - analysis; glycogen phosphorylase; hexokinase; Hexokinase - analysis; Humans; Invertebrates; Keto Acids; Lyases - analysis; Mammals; Muscle tissue; Muscles - enzymology; Myocardium - enzymology; Phosphorylases - analysis; Phosphotransferases - analysis; Species Specificity; triosephosphate dehydrogenase; Vertebrates; citrate synthase; adenylate kinase; 3-hydroxyacyl-CoA dehydrogenase; constant-proportion enzyme groups and metabolic correlations; triosephosphate dehydrogenase; creatine kinase; energy-supplying metabolism; Muscle tissue; comparative enzymology; glycogen phosphorylase; hexokinase
• ISSN: 0305-0491
• DOI: 10.1016/0305-0491(72)90116-2

1. 1. A comparative enzymological study was performed in order to examine whether constant proportions of certain key enzymes in energy-supplying metabolism in muscle represent a general principle of organization. For this purpose we studied fifty-one different types of muscle from vertebrates and avertebrates. 2. 2. Tight linear correlations exist between the activities of glycogen phosphorylase and triosephosphate dehydrogenase; of 3-hydroxy-acyl-CoA dehydrogenase and citrate synthase and of hexokinase and citrate synthase. 3. 3. In muscles containing creatine kinase, a linear correlation exists between the activity of this enzyme and of triosephosphate dehydrogenase. 4. 4. These findings can be interpreted as correlations of those metabolic systems being represented by the enzymes examined.