论文信息 - Ultrastructure studies on the binding of creatine kinase and the 165,000 molecular weight component to the M-band of muscle. - 字舞流文

Ultrastructure studies on the binding of creatine kinase and the 165,000 molecular weight component to the M-band of muscle.

C. Kay | R. Mani | R. Bradley | D. Scraba | O. S. Herasymowych

[1] 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.

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

[3] 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.

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

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

[6] 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.

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

[8] G. G. Knappeis,et al. THE ULTRASTRUCTURE OF THE M LINE IN SKELETAL MUSCLE , 1968, Journal of Cell Biology.

[9] F. Pepe. SOME ASPECTS OF THE STRUCTURAL ORGANIZATION OF THE MYOFIBRIL AS REVEALED BY ANTIBODY-STAINING METHODS , 1966, The Journal of cell biology.