[Diagnostic value of examining the composition of hemoglobin in hypothyroidism in children].
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Adolescent↗
Biomedical subjects
A L Solov'ev
Publications and source records attributed to A L Solov'ev.
[Electrophoretic study of muscle extracts of low ionic strength].
The method of Na-dodecylsulfate electrophoresis in polyacrylamide gel demonstrated that the so-called tonoactomyosin of smooth muscles extracted from the muscle homogenate with salt media of low ionic power represented a complicated protein system into whose composition there was included a heavy myosin chain with the mol wt of 210000, premyosin subunit with the mol wt of 230000, actin, and, possibly, a number of other proteins. The extracts of low ionic power possessed Mg2+ and Ca2+ activated by ATP-ase activity. The premyosin subunit was also revealed in the extracts of low ionic power from the skeletal muscle homogenates. It is supposed that premyosin subunit was included into the enzymatic system responsible for the ATP-asic properties of the extracts of low ionic power from the homogenates of different types of muscles.
Actomyosin↗
[Age peculiarities of actin polymerization in calves].
Studies have been made on the developmental changes in the polymerization degree of unfractionated actin extracts from skeletal muscles of 3-8-month calf embryos and adult cattle. It was shown that during the development, the polymerization capacity of actin increases, the increase being accompanied by a significant rise in the molecular weight of the protein. The pattern of age changes in the degree of polymerization of actin is similar to that in the molecular weight of actomyosin. Differences in fractional composition of actin extracts from skeletal muscles at various stages of embryonic development were observed. These differences may be responsible for age peculiarities of actin polymerization and may be associated with the formation of contractile activity in ontogenesis.
Actins↗
[Age peculiarities of actomyosin enzymic properties in embryogenesis].
Age changes in the subunits composition were comparatively studied for protein, ATPase activity, sensitivity to Ca2+ in low concentrations and alkaline activation of ATPase of natural actomyosin of skeletal muscles and myocardium in cattle feti. A rise in values in the process of the mentioned parameters development is established for actomyosin of skeletal muscles. The rise is especially considerable by the end of embryonic development. Correspondingly the myocardium actomyosin possesses a lower ATPase activity and higher sensitivity to Ca2+ in low concentrations. The ATPase activity rises moderately with development.
Actomyosin↗