Carbon-2 proton exchange at histidine-41 in bovine erythrocyte superoxide dismutase
- 1 September 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 165 (3) , 587-589
- https://doi.org/10.1042/bj1650587
Abstract
The C-2 proton of one histidine residue in bovine erythrocyte superoxide dismutase is shown to be particularly labile. This residue is identified by tritiation, protein digestion and subsequent peptide ‘mapping’ as histidine-41. A half-life for the exchange of histidine C-2 1H for 2H in 2H2O as solvent, at pD 8.1 and 40 degrees C, is estimated as approx. 9.2h, by 1H nuclear-magnetic-resonance spectroscopy.This publication has 6 references indexed in Scilit:
- The pH dependence of tritium exchange with the C-2 protons of the histidines in bovine trypsinBiochemistry, 1976
- Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignmentsBiochemistry, 1975
- Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands.Proceedings of the National Academy of Sciences, 1975
- Bovine erythrocyte superoxide dismutase. Complete amino acid sequence.1974
- Determination of pKa's of individual histidine residues in pancreatic ribonuclease by hydrogen-tritium exchange.1974
- Bovine Erythrocyte Cupro‐Zinc ProteinEuropean Journal of Biochemistry, 1971