Abstract
Summary
The kinetics of synthesis and degradation of aspartate aminotransferase (EC 2.6.1.1) isozymes were investigated in peripheral red blood cells of rats made reticulocytotic with phenylhydrazine. Immunochemical studies showed that reticulocytes contain predominantly the cationic isozyme, whereas mature erythrocytes contain only the anionic isozyme. Following initiation of phenylhydrazine treatment, the cationic isozyme increased 47-fold above its control level on Day 5, and the anionic isozyme increased threefold above its control level on the 8th day. The half-lives were 24.6 and 154.9 hr for the cationic and anionic isozyme, respectively. The faster turnover of the cationic isozyme appears to be related to its rapid rate of degradation.
We thank Miss Frances Grainger for her excellent technical assistance.
Get full access to this article
View all access options for this article.