Iodide quenching of tryptophan fluorescence in phosphorylase kinase
- 31 December 1977
- journal article
- Published by Elsevier in International Journal of Biochemistry
- Vol. 8 (5) , 369-372
- https://doi.org/10.1016/0020-711x(77)90007-6
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Regulation of muscle phosphorylase b kinase activity by inorganic phosphate and calcium ionsBiochemical Journal, 1974
- Fluorescence Quenching, a Tool for Probing Conformational Changes in Glycogen PhosphorylaseCanadian Journal of Biochemistry, 1973
- The Subunit Structure of Rabbit‐Skeletal‐Muscle Phosphorylase Kinase, and the Molecular Basis of Its Activation ReactionsEuropean Journal of Biochemistry, 1973
- Physicochemical properties of rabbit skeletal muscle phosphorylase kinaseBiochemistry, 1973
- Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ionBiochemistry, 1971
- Fluorescence quenching and conformational changes of proteinsBiochemical and Biophysical Research Communications, 1970
- The selective quenching of tryptophan fluorescence in proteins by iodide ion: Lysozyme in the presence and absence of substrateBiochemical and Biophysical Research Communications, 1967
- Activation of Skeletal Muscle Phosphorylase b Kinase by CA2+ *Biochemistry, 1964
- Purification and Properties of Rabbit Skeletal Muscle Phosphorylase b Kinase*Biochemistry, 1964
- THE ROLE OF METALS IN THE ACTIVATION OF MUSCLE PHOSPHORYLASEAnnals of the New York Academy of Sciences, 1960