Preparation and characterization of frog muscle myosin subfragment 1 and actin
- 1 April 1978
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 171 (1), 155-163
- https://doi.org/10.1042/bj1710155
Abstract
The preparation, structural and steady-state kinetic characteristics of contractile proteins from the leg muscle of frogs Rana temporaria and R. pipiens are described. Actin and myosin are indistinguishable. Proteins have structural and steady-state kinetic properties similar to those from rabbit fast-twitch skeletal muscle. Chymotrypsin digestion of frog myosin or myofibrils in the presence of EDTA yields subfragment 1, which is separated by chromatography into 2 components that are distinguished by their alkali L chain content.This publication has 29 references indexed in Scilit:
- Reaction mechanism of the magnesium ion-dependent adenosine triphosphatase of frog muscle myosin and subfragment 1Biochemical Journal, 1978
- Transient phase of adenosine triphosphate hydrolysis by myosin, heavy meromyosin, and subfragment 1Biochemistry, 1977
- The location of the divalent metal binding sites and the light chain subunits of vertebrate myosinBiochemistry, 1977
- Energetics and mechanism of actomyosin adenosine triphosphataseBiochemistry, 1976
- Intermediate states of actomyosin adenosine triphosphataseBiochemistry, 1976
- The magnesium-ion-dependent adenosine triphosphatase of bovine cardiac Myosin and its subfragment-1Biochemical Journal, 1976
- Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperatureNature, 1975
- Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosinNature, 1975
- DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTIONJournal of Biological Chemistry, 1949
- Studies on the composition and polymerization of actin.1948