ADP binds similarly to rigor muscle myofibrils and to actomyosin-subfragment one
نویسندگان
چکیده
منابع مشابه
Regulation of binding of subfragment 1 in isolated rigor myofibrils
A steric-hindrance model has been used to explain the regulation of muscle contraction by tropomyosin-troponin complex. The regulation of binding was studied by microscopic observation of mixtures of fluorescent subfragment 1 (S1) with rigor myofibrils at different actin-to-S1 ratios and in the presence and absence of calcium. Procedures were adapted to protect the critical thiols of S1 before ...
متن کاملADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle.
The rate constant for dissociation of ADP from actomyosin subfragment 1 (S1) has been measured in this laboratory and elsewhere for a variety of vertebrate muscle types. We have made the following observations: (i) In solution, the dissociation of ADP from actomyosin-S1 limits the rate of dissociation of actomyosin-S1-ADP by ATP and, presumably, also limits the rate of crossbridge detachment in...
متن کاملPolarization of fluorescently labeled myosin subfragment-1 fully or partially decorating muscle fibers and myofibrils.
Fluorescently labeled myosin heads (S1) were added to muscle fibers and myofibrils at various concentrations. The orientation of the absorption dipole of the dye with respect to the axis of F-actin was calculated from polarization of fluorescence which was measured by a novel method from video images of muscle. In this method light emitted from muscle was split by a birefringent crystal into tw...
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Bovine semitendinosus muscles were sampled immediately after death, after 24 hr postmortem with storage at 2 degrees , 16 degrees , or 37 degrees C, and after 312 hr postmortem with storage at 2 degrees and 16 degrees C. A biopsy technique was used to prevent shortening during glutaraldehyde fixation. Postfixation in osmium tetroxide was followed by embedding in an Epon-Araldite mixture. Bovine...
متن کاملProtein fluorescence changes associated with ATP and adenosine 5'-[gamma-thio]triphosphate binding to skeletal muscle myosin subfragment 1 and actomyosin subfragment 1.
1. The fluorescence changes accompanying the binding of ATP and adenosine 5'-[gamma-thio]triphosphate (ATP gamma S) to myosin subfragment 1 (S1) and actomyosin subfragment 1 (actoS1) have been reinvestigated at 20 degrees C and 1 degree C, pH 7.0, 0.1 M-KCl. 2. Two successive fluorescence enhancements are observed following ATP binding to both S1 and actoS1. 3. The slow fluorescence change has ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1984
ISSN: 0014-5793
DOI: 10.1016/0014-5793(84)81067-4