Zobrazeno 1 - 10
of 38
pro vyhledávání: '"E V, Petushkova"'
Publikováno v:
Эндодонтия Today, Vol 19, Iss 3, Pp 148-152 (2021)
Aim. To assess the need for repeated endodontic treatment and to determine the possible reasons for the repeated revision of the root canals according to the archival material of the state polyclinic in the period 2015-2020.Materials and methods. Arc
Externí odkaz:
https://doaj.org/article/de1cf8fbaa514f4381c97b6b33c2b289
Publikováno v:
Proceedings of the International Scientific Conference "Far East Con" (ISCFEC 2020).
Autor:
G M, Pronko, E V, Petushkova
Publikováno v:
Biokhimiia (Moscow, Russia). 56(3)
It was shown that the highly purified monoaldehyde derivative of ADP obtained by partial reduction of the dialdehyde derivative of ADP causes strong irreversible inhibition of the Ca-ATPase activity of myosin subfragment I, the inhibiting effect bein
Publikováno v:
Sovetskaia meditsina. (3)
Publikováno v:
Biokhimiia (Moscow, Russia). 49(11)
A comparative study of kinetic parameters (Km and V) of hydrolysis by heavy meromyosin of several synthetic ATP analogs with substituents at positions N(1) and N(C6) of the purine ring was carried out. Analysis of changes in the Km values suggests th
Autor:
V M, Kodentsova, E V, Petushkova
Publikováno v:
Nauchnye doklady vysshei shkoly. Biologicheskie nauki. (1)
Autor:
T I, Vlasova, E V, Petushkova
Publikováno v:
Biokhimiia (Moscow, Russia). 41(4)
The increase in temperature leads to a decrease in pKa of the group responsible for the activation of CaATP2- hydrolysis by myosin in the alkaline zone of pH. At 20-25 degrees the pKa value is about 9. The value of ionization heat (deltaHi) calculate
Publikováno v:
Biokhimiia (Moscow, Russia). 50(9)
It was demonstrated that the dialdehyde derivative of ATP is a good substrate for Ca-ATPase of heavy meromyosin (Km = (1.2-1.4) X 10(-4) M; V = VATP). At the same time, this compound can induce irreversible inhibition of the enzyme. Since oxo-ATP is
Autor:
E V, Petushkova, V M, Kodentsova
Publikováno v:
Biokhimiia (Moscow, Russia). 47(3)
The effects of several phosphorylating and alkylating analogs of the substrate on the ATPase activity of myosin and heavy meromyosin were compared. The data obtained confirmed the previously made assumption on the existence of two types of substrate-
Autor:
E V, Petushkova, T K, Semina
Publikováno v:
Biokhimiia (Moscow, Russia). 42(12)
Curves of V pH-dependence for Ca ATPase of myosin and heavy meromyosin are demonstrated to be well modelled with theoretical curves for the case of proton dissociation at three groups of enzyme-substrate complex with the loss of the activity at some