Zobrazeno 1 - 8
of 8
pro vyhledávání: '"S. V. Lepeshkevich"'
Autor:
N. V. Belko, V. N. Chizhevsky, M. V. Parkhats, S. V. Lepeshkevich, T. A. Kulahava, D. S. Mogilevtsev
Publikováno v:
Journal of Applied Spectroscopy. 90:316-324
Publikováno v:
Journal of Applied Spectroscopy. 90:265-273
Publikováno v:
Russian Physics Journal. 63:1359-1362
The paper is devoted to time-resolved studies of human hemoglobin, including excited electronic states and relaxation processes, quantum yield and dissociation electronic state, geminate rebinding stages and O2 escape from the protein matrix to a sol
Publikováno v:
High Energy Chemistry. 52:45-51
Cytochrome c oxidase, the key bioenergetic protein, was studied by femtosecond absorption spectroscopy. Time-resolved spectral characteristics of the difference spectra recorded in the timescale from 80 fs to 20 ps were analyzed. Electronic relaxatio
Autor:
S. V. Lepeshkevich, B. M. Dzhagarov
Publikováno v:
High Energy Chemistry. 44:127-129
The results of a pico- and nanosecond laser absorption spectroscopy study of the rebinding of the oxygen molecule by the triliganded hemoglobin tetramer in the R-state are presented.
Publikováno v:
High Energy Chemistry. 34:251-255
Hemoglobin molecules were studied by stationary and time-resolved laser absorption spectroscopy. On the basis of these results, the kinetic parameters of oxygenation in the course of methemoglobin formation under the combined action of radiation and
Publikováno v:
Biochemistry. Biokhimiia. 68(5)
Bimolecular oxygenation of tri-liganded R-state human hemoglobin (HbA) is described by bi-exponential kinetics with association rate constants k(alpha) = 27.2 +/- 1.3 (micro M*sec)(-1) and k(beta) = 62.9 +/- 1.6 (micro M*sec)(-1). Both the observed p
Publikováno v:
Ukrains'kyi biokhimichnyi zhurnal (1999 ). 73(3)
gamma-Irradiation has been defined to increase in the rats blood the methemoglobin level providing for shortening the initiation phase and accelerates the autocatalytic phase initiation, reduces the period of half transforming hemoglobin into methemo