PURIFIED MUSCLE PROTEINS AND THE WALKING RATE OF ANTS
- 1 June 1959
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 45 (6) , 785-791
- https://doi.org/10.1073/pnas.45.6.785
Abstract
The rate of hydrolysis of adenosine triphosphate (ATP) added to a purified protein system of actomyosin obtained from rabbit skeletal muscle or reconstituted actin and myosin obtained separately was measured over a temperature range from 300to 00C. By maintaining a low ionic strength it was possible to demonstrate that superprecipitation occurred over the entire temperature range. Approximately linear curves were obtained at the higher and lower temperatures and the calculated activation energies were 12 kcal and 25 kcal with a rapid transition occurring at about let from one linear phase to the other. Comparison of the data for the myosin and actomyosin catalyzed hydrolysis and the data for ant walking lead to the conclusion that the rate limiting reaction in the walking rate of ants is the hydrolysis of ATP catalyzed by actomyosin.This publication has 6 references indexed in Scilit:
- The stimulation of the adenosinetriphosphatase activities of myofibrils and l-myosin by 2:4-dinitrophenolBiochimica et Biophysica Acta, 1955
- Die erhöhung der rate der ATP-spaltung durch myosin- und actomyosin-gele bei beginn der spaltungBiochimica et Biophysica Acta, 1954
- Muscle Contraction and Fibrous Muscle ProteinsAdvances in Protein Chemistry, 1952
- ENZYME KINETICS AND THE RATE OF BIOLOGICAL PROCESSESThe Journal of general physiology, 1950
- On the Possibility of Identifying Chemical Processes in Living MatterProceedings of the National Academy of Sciences, 1924
- Thermokinetics of Liometopum Apiculatum MayrProceedings of the National Academy of Sciences, 1920