pH-dependent cold libility of rabbit skeletal muscle AMP deaminase
- 1 February 1983
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 742 (3), 623-629
- https://doi.org/10.1016/0167-4838(83)90281-9
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Regulation of skeletal muscle AMP deaminase effects of limited proteolysis on the activity of the rabbit enzymeFEBS Letters, 1979
- Negative homotropic cooperativity in rat muscle AMP deaminaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1979
- Effect of protons on the potassium(1+) ion activation of adenosine-5'-monophosphate aminohydrolaseBiochemistry, 1977
- Analysis of the cold lability behavior of rabbit muscle phosphofructokinaseBiochemical and Biophysical Research Communications, 1975
- AMP deaminase from rabbit skeletal muscle: The effect of monovalent cations on catalytic activity and molecular weightBiochimica et Biophysica Acta (BBA) - Enzymology, 1972
- 5′-Adenosine Monophosphate AminohydrolasePublished by Elsevier ,1971
- Protein-Protein Interaction and Enzymatic ActivityAnnual Review of Biochemistry, 1971
- Muscle AMP aminohydrolase. I. Some regulatory properties of rat skeletal muscle enzymeBiochimica et Biophysica Acta (BBA) - Enzymology, 1968
- Time dependence of activation of muscle AMP‐aminohydrolase by substrate and potassium ionFEBS Letters, 1968
- Über fermentative Desaminierung im Muskel.Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1928