Inactivation of skeletal muscle actin from newborn and adult rabbits in different conditions of polymerization and sample storage

Changes in polymerization degree of actin of newborn and adult rabbit muscles while storing solutions were studied. It is found that under different polymerization and storage conditions including the presence of ATP, Ca++ ions, 2-metacaptoethanole of ethanole which slow down the inactivation of act...

Full description

Saved in:
Bibliographic Details
Published inBiofizika Vol. 21; no. 3; p. 495
Main Authors Khaĭtlina, S Iu, Pinaev, G P
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.05.1976
Subjects
Actins
Adenosine Triphosphate
Aging
Animals
Calcium
Drug Storage
Ethanol
In Vitro Techniques
Mercaptoethanol
Polymers
Rabbits
Online AccessGet more information

Cover

More Information
Summary:Changes in polymerization degree of actin of newborn and adult rabbit muscles while storing solutions were studied. It is found that under different polymerization and storage conditions including the presence of ATP, Ca++ ions, 2-metacaptoethanole of ethanole which slow down the inactivation of actin the latter proceeds faster in newborn rabbits than in adult ones. It is suggested that with different inactivation rate of actin of newborn and adult rabbits are associated the differences in their polymerization degree found earlier.
ISSN:0006-3029