Adenylate kinase from rat liver: Molecular properties and structural comparison with yeast enzyme.
- 1 January 1985
- journal article
- research article
- Published by Japanese Society of Veterinary Science in The Japanese Journal of Veterinary Science
- Vol. 47 (1) , 63-72
- https://doi.org/10.1292/jvms1939.47.63
Abstract
Adenylate kinase from rat liver was found to have a MW in the range between 25,000 and 33,000 by sodium dodecylsulfate (SDS) polyacrylamide gel electrophoresis using the continuous and discontinuous buffer systems, sedimentation equilibrium, and Sephadex G-100 gel filtration. The purified enzyme was separated into 3 peaks of activities with isoelectric points (pl) of 8.1, 7.5 and 6.7, respectively, by column isoelectric focusing, and this heterogeneity may be due to deamidation. The purified enzyme has 1 disulfide bond which related to the active conformation of the enzyme and 2 SH groups which did not contribute to the enzyme activity. Antibody against the purified rat liver adenylate kinase showed a cross-reactivity with yeast adenylate kinase, but antibody against the rat muscle isoenzyme showed no cross-reactivity with the yeast enzyme. Apparently, antibody against the yeast enzyme cross-reacted with the rat liver isoenzyme but not with the rat muscle isoenzyme. These results indicate that there is a structural resemblance between the rat liver and yeast enzymes.This publication has 0 references indexed in Scilit: