作者: Hitoshi Ueno , William F. Harrington
DOI: 10.1016/0022-2836(86)90076-8
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摘要: Abstract Local melting within the subfragment-2 region of activated rabbit skeletal glycerinated muscle fibers has been investigated over temperature range 5 to 37 °C, using an enzyme (chymotrypsin)-probe method. The cleavage rates were determined from time-course formation digestion products by electrophoresis on sodium dodecyl sulfate-containing polyacrylamide gels. We found sites be localized in a restricted M r = 64,000 90,000/polypeptide chain, measured C terminus myosin rod (the hinge domain). rate constant for presence ATP-regenerating system was about 100 times larger at each than that rigor or relaxed and showed marked increase magnitude with increasing temperature. Comparative plots apparent rate-constant domain isometric force generated active versus MgATP concentration gave closely similar profiles suggesting strong positive correlation. Thus, there appears close coupling between conformational transition contractile when cross-bridges undergo cycling.