Phosphorus-31 nuclear magnetic resonance spectroscopy reveals two conformational forms of chloroacetol phosphate-bound triosephosphate isomerase
- 1 December 1990
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 173 (2) , 736-740
- https://doi.org/10.1016/s0006-291x(05)80097-x
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-.ANG. resolution: implications for catalysisBiochemistry, 1990
- In vitro deamidation of human triosephosphate isomeraseArchives of Biochemistry and Biophysics, 1986
- 31P nuclear magnetic resonance titrations: Simultaneous evaluation of all pH‐dependent resonance signalsMagnetic Resonance in Chemistry, 1984
- Molecular basis for the accumulation of acidic isozymes of triosephosphate isomerase on agingMechanisms of Ageing and Development, 1981
- Spectrophotometric studies on the interaction between triose phosphate isomerase and inhibitorsBiochemical Journal, 1979
- Efficiency and Evolution of Enzyme CatalysisAngewandte Chemie International Edition in English, 1977
- Studies of the histidine residues of triose phosphate isomerase by proton magnetic resonance and x-ray crystallographyJournal of Molecular Biology, 1976
- Ligand binding and denaturation titration of free and matrix-bound triosephosphate isomerasesArchives of Biochemistry and Biophysics, 1975
- Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomeraseBiochemistry, 1971
- Haloacetol phosphates. Potential active-site reagents for aldolase, triose phosphate isomerase, and glycerophosphate dehydrogenase. I. Preparation and propertiesBiochemistry, 1970