Structural pattern of subfragment 1 of skeletal muscle myosin
نویسندگان
چکیده
منابع مشابه
Subunit interactions of skeletal muscle myosin and myosin subfragment 1. Evidence for heavy chain-alkali light chain association-dissociation equilibrium.
Modification of the free alkali light chains of myosin by iodoacetylation results in a much lower extent of exchange into myosin subfragment 1 by the thermal hybridization procedure (Burke, M., and Sivaramakrishnan, M. (1981) Biochemistry 20, 5908-5913). As reported by others (Wagner, P. D., and Stone, D. B. (1983) J. Biol. Chem. 258, 8876-8882), free alkali light chains modified by iodoacetate...
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This enzymatically active subunit of smooth muscle myosin has not so far been isolated. Previous work on cow carotid myosin [l] and on chicken gizzard myosin [2] has revealed that these myosins are, as cardiac myosin [3, cf. 4] much more resistant to tryptic digestion than rabbit skeletal myosin. Furthermore, if the L-meromyosin (LMM) obtained behaves on the whole similarly to its skeletal coun...
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The interdomain motions in myosin subfragment 1 (S1) were studied by steady-state and time-resolved fluorescence of tryptophan residues and N-(iodoacetyl)-N'-(5-sulfo-1-naphtyl)ethylenediamine (AEDANS) attached to Cys178 of alkali light chain 1 (A1) exchanged into S1. The efficiency of fluorescence resonance energy transfer (FRET) from tryptophan residues of motor domain to AEDANS at A1 decreas...
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 ...
متن کاملProtease-sensitive regions in myosin subfragment 1.
Proteolytic digestions of myosin subfragment 1 (S-1) with elastase, subtilisin, papain, thermolysin, and Staphylococcus aureus protease reveal that the two trypsin-sensitive regions in S-1 have broad protease susceptibility. The cleavage of S-1 by these enzymes yields products that correspond within 1-2 kilodaltons (kDa) to the 25-, 50-, and 20-kDa fragments produced by trypsin. Papain and ther...
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ژورنال
عنوان ژورنال: Biopolymers and Cell
سال: 1990
ISSN: 0233-7657,1993-6842
DOI: 10.7124/bc.000269