[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 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.
D000199:Actins; D000255:Adenosine Triphosphate; D000375:Aging; D000818:Animals; D002118:Calcium; D004356:Drug Storage; D000431:Ethanol; D066298:In Vitro Techniques; D008623:Mercaptoethanol; D011108:Polymers; D011817:Rabbits
D000199:Actins; D011108:Polymers; D000431:Ethanol; D008623:Mercaptoethanol; D000255:Adenosine Triphosphate; D002118:Calcium
Inaktivatsiia aktina skeletnykh myshts novorozhdennogo i vzroslogo krolika pri raznykh usloviiakh polimerizatsii i khraneniia preparatov