Properties of the tryptophan residue in rabbit liver microsomal cytochrome P-450 isozyme 2 as determined by fluorescence
- 1 April 1985
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 128 (2) , 676-682
- https://doi.org/10.1016/0006-291x(85)90099-3
Abstract
No abstract availableThis publication has 23 references indexed in Scilit:
- Oxygen Activation by Cytochrome P-4501Annual Review of Biochemistry, 1980
- Comparative study of two highly purified forms of liver microsomal cytochrome P-450: Circular dichroism and other propertiesArchives of Biochemistry and Biophysics, 1979
- Fluorescence studies of human growth hormoneBiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ionBiochemistry, 1971
- Studies of the location of tyrosyl and tryptophanyl residues in protein. II. Applications of model data to solvent perturbation studies of proteins rich in both tyrosine and tryptophanBiochemistry, 1968
- Fluorescence and protein structureBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- The ultraviolet fluorescence of proteins in neutral solutionBiochemical Journal, 1960
- Electronic energy transfer in haem proteinsDiscussions of the Faraday Society, 1959
- Photochemische spaltung des kohlenoxydmyoglobins durch ultraviolette strahlung (wirksamkeit der durch die proteinkomponente des pigments absorbierten quanten)Biochimica et Biophysica Acta, 1947
- Das sauerstoffübertragende Ferment der AtmungAngewandte Chemie, 1932