Fluorescence studies on the interaction of muscle M-line proteins, creatine kinase and the 165,000 dalton component, with each other and with myosin and myosin subfragments.

[1]  M. Steiner.  Flourescence studies of platelet tubulin. , 1980, Biochemistry.

[2]  C. Kay,et al.  Ultrastructure studies on the binding of creatine kinase and the 165,000 molecular weight component to the M-band of muscle. , 1980, Journal of molecular biology.

[3]  C. Kay,et al.  Physical, chemical and ultrastructural studies on muscle M-line proteins. , 1980, The International journal of biochemistry.

[4]  C. Kay,et al.  Spectrophotometric titration of muscle M-line proteins: creatine kinase and the 165,000 dalton protein component. , 1980, The International journal of biochemistry.

[5]  C. Kay,et al.  Interaction studies of the 165 000 dalton protein component of the M-line with the S2 subfragment of myosin. , 1978, Biochimica et biophysica acta.

[6]  C. Kay,et al.  Isolation, purification and characterization of creatine kinase from bovine cardiac muscle. , 1978, Biochimica et biophysica acta.

[7]  C. Kay,et al.  Isolation and characterization of the 165 000 dalton protein component of the M-line of rabbit skeletal muscle and its interaction with creatine kinase. , 1978, Biochimica et biophysica acta.

[8]  C. Heizmann,et al.  Isolation and characterization of glycogen phosphorylase b from chicken breast muscle: comparison with a protein extracted from the M. line. , 1978, The Journal of biological chemistry.

[9]  H. Eppenberger,et al.  Localization of creatine kinase isoenzymes in myofibrils. II. Chicken heart muscle , 1977, The Journal of cell biology.

[10]  J. Trinick,et al.  M-protein from chicken pectoralis muscle: isolation and characterization. , 1977, Journal of molecular biology.

[11]  C. Kay,et al.  Physicochemical studies on the creatine kinase M-line protein and its interaction with myosin and myosin fragments. , 1976, Biochimica et biophysica acta.

[12]  A. Wang,et al.  Electron paramagnetic resonance and nanosecond fluorescence depolarization studies on creatine-phosphokinase interaction with myosin and its fragments. , 1975, Journal of supramolecular structure.

[13]  T. Houk,et al.  Location of the creatine phosphokinase binding site of myosin. , 1973, Biochemical and biophysical research communications.

[14]  K. Morimoto,et al.  Isolation and physical chemical properties of an M-line protein from skeletal muscle. , 1972, The Journal of biological chemistry.

[15]  W. O'Sullivan.  The reaction of creatine kinase with dithiobisnitrobenzoic acid. Formation of derivatives of the enzyme. , 2009, International journal of protein research.

[16]  M. Morales,et al.  Studies of myosin conformation by fluorescent techniques. , 1969, Biochemistry.

[17]  R. Cowgill.  Fluorescence and protein structure. XV. Tryptophan fluorescence in helical muscle protein. , 1968, Biochimica et biophysica acta.

[18]  G. Edelman,et al.  Fluorescent probes for conformational states of proteins. II. The binding of 2-p-toluidinylnaphthalene-6-sulfonate to alpha-chymotrypsin. , 1967, Biochemistry.

[19]  G. Edelman,et al.  Fluorescent probes for conformational states of proteins. I. Mechanism of fluorescence of 2-p-toluidinylnaphthalene-6-sulfonate, a hydrophobic probe. , 1966, Biochemistry.

[20]  G. Weber,et al.  Chapter 17 – Interaction of Proteins with Radiation , 1965 .

[21]  K. Yagi,et al.  Coupled reaction of creatine kinase and myosin A-adenosine triphosphatase. , 1962, The Journal of biological chemistry.