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Literature DB >> 651

The relation between myosin adenosinetriphosphatase activity and inactivation of myosin under alkaline conditions of heart muscles in mammals of different size.

Abstract

ATPase activity of myosin in the heart muscle of the mouse, rat, guinea-pig, rabbit and pig was studied at neutral pH and under mild alkaline conditions. At neutral pH the ATPase activity of myosin is inversely related to body size of the animal species. The decrease of ATPase activity of myosin after alkaline preincubation depends on the degree of ATPase activity of intact myosin, i.e. myosin from the heart of the mouse exhibits high ATPase activity ae same relationship was found, when comparing myosin of new-born and adult heart muscle. It is concluded that the rate of alkaline inactivation of heart myosin is directly related to the degree of ATPase activity of intact myosin in all animals.

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Year: 1975 PMID： 651 DOI： 10.1007/BF00583523

Source DB: PubMed Journal: Pflugers Arch ISSN： 0031-6768 Impact factor: 3.657

11 in total

1. MYOSIN OF FAST AND SLOW MUSCLES OF THE RABBIT.

Authors: M BARANY; K BARANY; T RECKARD; A VOLPE
Journal: Arch Biochem Biophys Date: 1965-01 Impact factor: 4.013

2. Studies on myosin from red and white skeletal muscles of the rabbit. II. Inactivation of myosin from red muscles under mild alkaline conditions.

Authors: J C Seidel
Journal: J Biol Chem Date: 1967-12-10 Impact factor: 5.157

3. The design of muscles.

Authors: A V HILL
Journal: Br Med Bull Date: 1956-09 Impact factor: 4.291

4. Myosin and adenosinetriphosphatase.

Authors: K Bailey
Journal: Biochem J Date: 1942-02 Impact factor: 3.857

5. The relation between ATPASE activity and light chains of myosin in developing, adult and denervated muscles of several animals species.

Authors: I Syrový
Journal: Physiol Bohemoslov Date: 1976

6. Studies on myosin from red and white skeletal muscles of the rabbit. I. Adenosine triphosphatase activity.

Authors: F A Sreter; J C Seidel; J Gergely
Journal: J Biol Chem Date: 1966-12-25 Impact factor: 5.157

Review 7. Dynamic properties of mammalian skeletal muscles.

Authors: R I Close
Journal: Physiol Rev Date: 1972-01 Impact factor: 37.312

8. Differences between slow and fast muscle myosin. Adenosine triphosphatase activity and release of associated proteins by p-chloromercuriphenylsulfonate.

Authors: F J Samaha; L Guth; R W Albers
Journal: J Biol Chem Date: 1970-01-25 Impact factor: 5.157

The relation between myosin adenosinetriphosphatase activity and inactivation of myosin under alkaline conditions of heart muscles in mammals of different size.

1. MYOSIN OF FAST AND SLOW MUSCLES OF THE RABBIT.

2. Studies on myosin from red and white skeletal muscles of the rabbit. II. Inactivation of myosin from red muscles under mild alkaline conditions.

3. The design of muscles.

4. Myosin and adenosinetriphosphatase.

5. The relation between ATPASE activity and light chains of myosin in developing, adult and denervated muscles of several animals species.

6. Studies on myosin from red and white skeletal muscles of the rabbit. I. Adenosine triphosphatase activity.

Review 7. Dynamic properties of mammalian skeletal muscles.

8. Differences between slow and fast muscle myosin. Adenosine triphosphatase activity and release of associated proteins by p-chloromercuriphenylsulfonate.

9. Myosin from fast and slow skeletal and cardiac muscles of mammals of different size.

10. ATPase activity of myosin correlated with speed of muscle shortening.

1. Atrial and ventricular myosin ATPase--divergence with increasing animal species size.

2. Myosin types and fiber types in cardiac muscle. I. Ventricular myocardium.