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Biomedical subjects

Iu Sh Moshkovskiĭ

Publications and source records attributed to Iu Sh Moshkovskiĭ.

At least 19 recordsLinked to original sources
PubMed1987

[Effect of actoprotectors on Ca, Mg-dependent ATPase activity in the sarcoplasmatic reticulum of rabbit muscles].

The effect of different chemical compounds on Ca, Mg-dependent ATPase (Ca-ATPase) sarcoplasmic reticulum (SR) hydrolytic activity as well as their actoprotecting (AP) activity, the ability to increase organism's resistance under muscle stress and antihypoxanthic (AH) activity to increase the organism's survival under conditions of low pressure has been studied. The compounds with AP-activity have been shown to be strong inhibitors of Ca-ATPase SR hydrolytic activity. No correlation between AP-activity of the compounds and their effect on Ca-ATPase SR has been found. The membranotropic activity of actoprotectors has been shown by electronic paramagnetic resonance method. A suggestion has been made to use Ca-ATPase SR as a tested object during the forecasting actoprotecting activity of new chemical compounds.

Adaptation, Physiological↗
PubMed1978

[Induction of a menadione-dependent respiratory shunt by a platinum complex].

Submitochondrial particles (SMP) from the bovine heart were treated with platinum complex--K [C2H4 PtCl3] (Zeize's salt); there occurred a menadion-dependent shunt, this being expressed in menadion stimulation of oxygen consumption under conditions of electron transport block with rotenon. This effect was observed only with the use in the capacity of a substrate of NAD.N2, but not of succinate. Menadion-dependent respiration induced with Zeize's salt was dicoumarol-sensitive, but was not inhibited by antimycin and cyanide, this differentiating it from menadionreductase shunt in the intact hepatic mitochondria.

Animals↗
PubMed1975

[Effect of palladium and platinum salts on bacteriophage T4 and its isolated DNA].

The effect of palladium and platinum salts (K2PdCl4, K2PtCl4) on bacteriophage F4 and its isolated DNA in genetic transformation is investigated. Both compounds efficiently inactivated the phage and decreased the transforming activity of donor DNA. The palladium salt exhibited the higher activity. The palladium compounds inhibited the transforming activity of native donor DNA to a greater degree. No difference was observed in the degree of inactivation of the transforming activity of native and denatured DNA under the effect of platinum salt. It is suggested that the difference in the transforming activity of donor DNA treated with the tested compounds reflect the pattern of their interactions with nucleic acids.

Coliphages↗
PubMed1975

[Study of the interaction of human serum albumin with penicillins by means of spin labels].

Interaction of 8 penicillin preparations with human serum albumin was studied with the spin-labels method and a probe. Correlation between the binding level of penicillins with human serum albumin and their effect on the spectrum of EPR of the spin-label attached to albumin was observed only with the use of a hydrophobic probe (radical III). The covalent attached marks and the hydrophobic probe may be used for rapid orienting estimation of pencillin interaction with albumin.

Ampicillin↗
PubMed1966

[DNA cryolysis].

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Animals↗
PubMedDate not supplied

[Interaction of pancreatic RNAase A with platinum ions].

Complex formation between RNAase and Pt(II) has been studied by gel filtration and conductometry, and spectrophotometry. Existence of three strong binding locations with the binding location of 2 times 10-4 M-1 has been stated. Effect of Pt(II) on hydrolase activity of RNAase Ahas been investigated. An inhibiting effect showed itself at high concentrations of platinum ions. A conclusion has been made concerning the nature of groups participating in complex formation with Pt(II). Modification of three methionin residues does not influence the enzyme activity at 24-48 hour preincubation.

Binding Sites↗
PubMedDate not supplied

[Interaction of platinum and palladium complexes with thiol groups of Ca2+-dependent ATPase from sarcoplasmic reticulum].

In native preparations of sarcoplasmic reticulum 10-12 thiol groups (in g-eqv per 10(5) g of protein) were estimated by the Benesh method (titration with AgNO3) and 2 thiol groups--by Ellman (titration with dithionitrobenzoic acid). After denaturation of the sarcoplasmic reticulum preparations with 8 M urea 10-12 thiol groups were also determined by the Ellman method. When the preparations were treated with platinum tetrachloride or with palladium diaminodichloride, only 3 thiol groups were estimated by the Benesh and no one - by the Ellman method. Platinum and palladium complexes inhibited also the Ca2+-dependent activity blocking the transport of Ca2+ in sarcoplasmic reticulum. The inhibition was partially removed by glutathione.

Adenosine Triphosphatases↗