Internal Structure of Myosin Subfragment-1 (S-1) Molecule
نویسندگان
چکیده
منابع مشابه
Subfragment 1 of cow carotid myosin.
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 کاملBinding of myosin subfragment-1 to F-actin.
During a part of the hydrolytic cycle, myosin head (S1) carries no nucleotide and binds strongly to an actin filament forming a rigor bond. At saturating concentration of S1 in rigor, S1 is well known to form 1:1 complex with actin. However, we have provided evidence that under certain conditions S1 could also form a complex with 2 actin monomers in a filament (Andreev, O.A. & Borejdo, J. (1991...
متن کاملTwo different rigor complexes of myosin subfragment 1 and actin.
Our previous titration and cross-linking experiments showed that myosin subfragment 1 (S1) can bind to one or two monomers in F-actin [Andreev, O. A., & Borejdo, J. (1991) Biochem. Biophys. Res. Commun. 177, 350-356; (1992a) J. Muscle Res. Cell Motil. 13, 523-533; (1992b) Biochem. Biophys. Res. Commun. 188, 94-101]. In the present work we used a sedimentation method to extend these studies to e...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1981
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.21.219