Effects of Anions on the Substrate Affinities of the Pyridoxal and Pyridoxamine Forms of Mitochondrial and Supernatant Aspartate Transaminases
Open Access
- 1 June 1971
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 246 (11) , 3623-3630
- https://doi.org/10.1016/s0021-9258(18)62174-x
Abstract
No abstract availableThis publication has 28 references indexed in Scilit:
- The molecular weight and subunits of the isozymes of glutamic aspartic transaminaseBiochemical and Biophysical Research Communications, 1970
- Enzymes Activated by Monovalent CationsScience, 1970
- Studies on succinate dehydrogenase. VI. Inhibition by monocarboxylic acidsBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- Spectrophotometric and kinetic evidence for the existence of at least two salt-dependent conformations of α-chymotrypsin at pH values near neutralityArchives of Biochemistry and Biophysics, 1969
- Mitochondrial aspartate transaminase. II. Isolation and characterization of the multiple formsBiochemistry, 1969
- Effects of phosphate and other anions on measurement of the activities of the isozymes of rat liver aspartate aminotransferaseAnalytical Biochemistry, 1968
- Pyridoxal PhosphateAnnual Review of Biochemistry, 1967
- Preparation of the phosphopyridoxamine form of the glutamic-aspartic transaminaseBiochemical and Biophysical Research Communications, 1966
- Multiple forms of supernatant glutamate-aspartate transaminase from pig heartBiochemical and Biophysical Research Communications, 1965
- Comparative Studies on Glutamic-Oxalacetic Transaminases from the Mitochondrial and Soluble Fractions of Mammalian TissuesPublished by Elsevier ,1964