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Biomedical subjects

M M Ogievetskaya

Publications and source records attributed to M M Ogievetskaya.

6 recordsLinked to original sources
PubMed1990

Investigation of the SOS response of Escherichia coli after gamma-irradiation by means of the SOS chromotest.

The kinetics of SOS system induction in Escherichia coli PQ37 cells by gamma-irradiation has been studied by the SOS chromotest technique. It was shown that the synthesis of constitutive alkaline phosphatase is not immediately stopped in cells that suffered lethal damages from gamma-irradiation. The production of DNA damages inducing the SOS system was 0.021/Gy per genome. The SOS system was switched off approximately 200 min after gamma-irradiation. A correction is proposed to the calculation of the SOS system induction factor.

Alkaline Phosphatase↗
PubMed1981

Trace elements in phasic and tonic muscles.

The differences in the content of trace elements (Fe, Cu, Zn, Br, Rb and Sr) in phasic and tonic scallop adductor muscles have been revealed by using X-ray fluorescence analysis. The phasic (yellow) muscles have been found to be richer in Fe and Cu while more deficient in Zn and Br as compared to the tonic (white) muscles. No appreciable differences in the Rb and Sr content has been found. A statistical treatment of the data obtained suggests that phasic and tonic muscles differ in their metabolism of trace elements and the regulation of the concentrations of various trace elements by the muscle cell is achieved by different mechanisms.

Animals↗
PubMed1977

Method for the determination of protein evolution rates by amino acid composition. Evolution rate of actins.

A method has been developed to determine the actin evolution rate. The method is based on amino acid compositon. The actin evolution rate has been established to be extremely low. Only three or less amino acid changes per hundred amino acid residues have accumulated for a 100 million years. One can explain the conservative nature of actin evolution as a sequence of its unique tightly fitted structure rich in biologically active centres at short distances from each other. The peculiar invariability of polar amino acids leads to a conclusion that some given distribution of charges is necessary for the unique functioning of actin molecules.

Actins↗