Synthetic Peptides Model Instability of Cardiac Myosin Subfragment-2
نویسندگان
چکیده
منابع مشابه
Bovine cardiac myosin subfragment 1. Transient kinetics of ATP hydrolysis.
The kinetics of binding and hydrolysis of ATP by bovine cardiac myosin subfragment 1 has been reinvestigated. More than 90% of the total fluorescence amplitude associated with ATP hydrolysis occurs with an apparent second-order rate constant of 8.1 X 10(5) M-1 S-1 and a limiting rate constant of approximately 140 S-1 (100 mM KCl, 50 mM 1,3-bis-[tris(hydroxymethyl)methylamino]-propane, 10 mM MgC...
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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...
متن کاملThe interdomain motions in myosin subfragment 1.
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 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...
متن کاملThe magnesium-ion-dependent adenosine triphosphatase of bovine cardiac Myosin and its subfragment-1.
The kinetics of the Mg2+-dependent ATPase (adenosine triphosphatase) activity of bovine cardiac myosin and its papain subfragment-1 were studied by using steady-state and pre-steady-state techniques, and results were compared with published values for the corresponding processes in the ATPase mechanism of rabbit skeletal-muscle myosin subfragment-1. The catalytic-centreactivity for cardiac subf...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2013
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2012.11.882