Zobrazeno 1 - 9
of 9
pro vyhledávání: '"M A, Ferenczi"'
Publikováno v:
Molekuliarnaia biologiia. 43(4)
The interference fine structure of the M3 reflection on the low-angle x-ray diffraction patterns of muscle fibres is used for the measurements of axial movements of myosin heads with a precision of 0.1-0.2 nm. We have measured changes in the M3 inter
Publikováno v:
Advances in experimental medicine and biology. 453
Muscle proteins utilise the hydrolysis of ATP to provide the energy for force development and the production of mechanical work. We have developed a technique with high sensitivity and time resolution to probe as directly as possible the link between
Publikováno v:
Biophysical journal. 68
A new method for the measurement of phosphate release in contracting and relaxed permeabilized muscle fibers is described. The assay is based on a genetically engineered phosphate-binding protein labeled with a coumarin fluorescent probe, which binds
Publikováno v:
Biochemical Journal. 171:155-163
The preparation, structural and steady-state kinetic characteristics of contractile proteins from the leg muscle of frogs Rana temporaria and Rana pipiens are described. Actin and myosin from the two frog species are indistinguishable. The proteins h
Autor:
R J, Barsotti, M A, Ferenczi
Publikováno v:
The Journal of biological chemistry. 263(32)
The kinetics of ATP hydrolysis and tension responses were studied simultaneously in a permeabilized preparation of cardiac tissue of the guinea pig. This was achieved by combining laserflash photolysis of P3-1-(2-nitrophenyl)ethyladenosine 5'-triphos
Autor:
M A, Ferenczi, C I, Spencer
Publikováno v:
Advances in experimental medicine and biology. 226
Caged-ATP (P3-1(2-nitrophenyl) ethyladenosine 5'-triphosphate) has been used to introduce millimolar concentrations of ATP rapidly into glycerinated muscle fibres, thus removing the limit imposed by diffusion to the time resolution of kinetic measure
Publikováno v:
The Journal of physiology. 292
Publikováno v:
Society of General Physiologists series. 37
Publikováno v:
The Biochemical journal. 171(1)
The Mg2+-dependent ATPase (adenosine 5′-triphosphatase) mechanism of myosin and subfragment 1 prepared from frog leg muscle was investigated by transient kinetic technique. The results show that in general terms the mechanism is similar to that of