Molecular Structure Analysis of Myosin Subfragment 1 for Evaluation of Kinetic Function.
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...
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1. The enthalpy changes during individual reaction steps of the myosin subfragment 1 ATPase were studied with the use of a new stopped-flow calorimeter [Howarth, Millar & Gutfreund (1987) Biochem. J. 248, 677-682]. 2. At 5 degrees C and pH 7.0, the endothermic on-enzyme ATP-cleavage step was observed directly (delta H = +64 kJ.mol-1). 3. ADP binding is accompanied by a biphasic enthalpy change....
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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: TRANSACTIONS OF THE JAPAN SOCIETY OF MECHANICAL ENGINEERS Series C
سال: 1997
ISSN: 0387-5024,1884-8354
DOI: 10.1299/kikaic.63.2402