Erythrocytes: 5′-Adenylic Acid Deaminase Requirement for Ammonia or Monovalent Metal Ion
- 5 July 1963
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 141 (3575), 44-45
- https://doi.org/10.1126/science.141.3575.44
Abstract
5'-Adenylic acid deaminase free from sodium and potassium ion is prepared from erythrocytes by a convenient method. Like adenosine triphosphatase and adenylic kinase from erythrocytes, the deaminase is activated by some monovalent cations, but unlike these enzymes it requires the presence of a monovalent cation. In all three instances the pattern of activation by ions is similar and suggests a common mechanism.Keywords
This publication has 9 references indexed in Scilit:
- Apparent uncoupling of the Na+ and K+ activation of the human erythrocyte membrane adenosine triphosphataseBiochimica et Biophysica Acta, 1963
- The asymmetrical stimulation of a membrane adenosine triphosphatase in relation to active cation transportBiochemical Journal, 1962
- Adenosinetriphosphatase activity and the active movements of alkali metal ionsThe Journal of Physiology, 1961
- Membrane Adenosine Triphosphatase as a Participant in the Active Transport of Sodium and Potassium in the Human ErythrocyteJournal of Biological Chemistry, 1960
- Further investigations on a Mg++ + Na+-activated adenosintriphosphatase, possibly related to the active, linked transport of Na+ and K+ across the nerve membraneBiochimica et Biophysica Acta, 1960
- DIFFERENTIAL SPECTROPHOTOMETRY OF PURINE COMPOUNDS BY MEANS OF SPECIFIC ENZYMESPublished by Elsevier ,1947
- DIFFERENTIAL SPECTROPHOTOMETRY OF PURINE COMPOUNDS BY MEANS OF SPECIFIC ENZYMES .2. DETERMINATION OF ADENINE COMPOUNDS1947
- Blood ammoniaBiochemical Journal, 1939