Formate-induced Labeling of the Active Site of Aspartate Aminotransferase by β-Chloro-l-alanine
Open Access
- 1 October 1974
- journal article
- Published by Elsevier
- Vol. 249 (20) , 6684-6692
- https://doi.org/10.1016/s0021-9258(19)42208-4
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Labeling of the active site of cytoplasmic aspartate aminotransferase by β-chloro-L-alanineBiochemical and Biophysical Research Communications, 1973
- Selective modification of the mitochondrial isozyme of aspartate aminotransferase by .beta.-bromopropionate. I. Inactivation process and properties of inactivated enzymeBiochemistry, 1972
- Selective modification of the mitochondrial isozyme of aspartate aminotransferase by β-bromopropionate. II. Chemical structure of the modified siteBiochemistry, 1972
- Evidence for the presence of a distinct subsite for binding the distal carboxyl group of dicarboxylate substrates and its role in the catalytic activity of aspartate aminotransferaseBiochemical and Biophysical Research Communications, 1972
- A comparative study on the affinity labelling of aspartate aminotransferase isozymes by β-bromopyruvateBiochemical and Biophysical Research Communications, 1970
- Reaction of L-serine O-sulfate with aspartate aminotransferaseBiochemistry, 1969
- The Reaction of β‐Chloroglutamic Acid with Glutamate‐Aspartate TransaminaseEuropean Journal of Biochemistry, 1968
- [54] l-Lactic dehydrogenase: Heart (H4)Published by Elsevier ,1966
- Crystallization of 2-oxoglutarate L-aspartate transaminases from mitochondrial and soluble fractions of beef liverBiochemical and Biophysical Research Communications, 1963
- Verwandlung des l‐Serins in d‐AlaninEuropean Journal of Inorganic Chemistry, 1907