Metal-tyrosyl interaction in carboxypeptidases: Phosphorescence studies
- 1 March 1975
- journal article
- Published by Wiley in FEBS Letters
- Vol. 51 (1) , 262-265
- https://doi.org/10.1016/0014-5793(75)80902-1
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Affinity labelling of carboxypeptidase B: Modification of a methionyl residueBiochemical and Biophysical Research Communications, 1974
- Chemical Approaches to the Mode of Action of Carboxypeptidase BIsrael Journal of Chemistry, 1974
- Metallocarboxypeptidases: A cadmium — Carboxypeptidase B with peptidase activityBiochemical and Biophysical Research Communications, 1973
- The Role of a Tyrosyl Residue in the Mechanism of Action of Carboxypeptidase B: Luminescence StudiesProceedings of the National Academy of Sciences, 1973
- Binding of the by-product analog benzylsuccinic acid by carboxypeptidase ABiochemistry, 1973
- Approach to inhibition kinetics. Measurement of enzyme-substrate complexes by electronic energy transferBiochemistry, 1972
- Differences between the Conformation of Arsanilazotyrosine 248 of Carboxypeptidase A in the Crystalline State and in SolutionProceedings of the National Academy of Sciences, 1971
- Structure and mechanism in the enzymic activity of carboxypeptidase A and relations to chemical sequenceAccounts of Chemical Research, 1970
- Metalloenzymes: the entatic nature of their active sites.Proceedings of the National Academy of Sciences, 1968
- Studies of the Triplet State of Proteins by Electron Spin Resonance Spectroscopy*Biochemistry, 1966