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1.
Biofizika ; 31(5): 842-4, 1986.
Artigo em Russo | MEDLINE | ID: mdl-3778960

RESUMO

It was shown by electron microscopic study that in the presence of inhibitor of myosin ATPase protein P55 the long fibrils of myosin became short.


Assuntos
Proteínas Musculares/análise , Miofibrilas/análise , Miosinas/análise , Sarcômeros/análise , Animais , Microscopia Eletrônica , Coelhos , Sarcômeros/ultraestrutura
2.
Tsitologiia ; 23(8): 901-6, 1981 Aug.
Artigo em Russo | MEDLINE | ID: mdl-7303157

RESUMO

The chromatin structure of Physarum polycephalum was studied with electron microscope at different phases of its mitotic cycle. At the S-phase and during mitosis, the chromatin has a nucleosomal structure. At the early G2-phase the chromatin structure changes, long regions of non-beaded structure being found in the chromatin fibers. At the late G2-phase, the major part of chromatin loses its globular organization, with chromatin fibres without a pronounced subunit structure prevailing in the preparations. Biochemical data show that the amount of chromatin resistant to staphylococcal nuclease varies during the mitotic cycle. The amount of nuclease-resistant chromatin is equal to 80% at the S-phase, to decrease up to 50-60% by the early G2-phase. Successive changes of chromatin structure at different levels of its transcriptional activity are found. Lability of nucleosomes is shown to increase with the increase in the transcriptional activity of chromatin, thus leading presumably to the chromatin structural alterations during the mitotic cycle.


Assuntos
Cromatina/ultraestrutura , Mitose , Physarum/ultraestrutura , Interfase , Microscopia Eletrônica
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