Zobrazeno 1 - 8
of 8
pro vyhledávání: '"M. V. Kovina"'
Publikováno v:
Детские инфекции (Москва), Vol 23, Iss 3, Pp 30-34 (2024)
Purpose of the study: to study the characteristics of physical development in 174 children with cerebral palsy using various rating scales (specialized centile tables, international standards of the World Health Organization, as well as regional tabl
Externí odkaz:
https://doaj.org/article/30b3b4361bab43d8ae5ffdfc1018b383
Publikováno v:
Cell and Tissue Biology. 7:136-139
Tissue renewal is a phenomenon based on replacement of vanishing cells by progeny of resident or circulated stem cells (SCs). The delivery of stem cells via circulation should result in stem-cell homing and differentiation into a wide variety of tiss
Publikováno v:
Tsitologiia. 54(12)
Tissue renewal is the known phenomenon, when the progeny of resident or circulated stem cells (SC) replaces the vanishing cells. The delivery of stem cells via circulation should result in stem cell homing and differentiation into wide variety of tis
Publikováno v:
Biochemistry. Biokhimiia. 66(8)
The interaction of transketolase ketosubstrates with the holoenzyme has been studied. On addition of ketosubstrates cleaving both irreversibly (hydroxypyruvate) and reversibly (xylulose 5-phosphate), identical changes in the CD spectrum at 300-360 nm
Publikováno v:
Biochemistry. Biokhimiia. 65(10)
Two substrates of the transketolase reaction are known to bind with the enzyme according to a ping-pong mechanism [1]. It is shown in this work that high concentrations of ribose-5-phosphate (acceptor substrate) compete with xylulose-5-phosphate (don
Publikováno v:
Biochemistry. Biokhimiia. 63(8)
The two-step mechanism of coenzyme (thiamine diphosphate, ThDP) binding with two initially identical active sites of apotransketolase has been examined with a kinetic model. Cooperativity between sites in the primary ThDP binding and in the following
Publikováno v:
Biochemistry. Biokhimiia. 62(4)
A kinetic model of bisubstrate reaction catalyzed by baker's yeast transketolase is proposed. The model considers individual stages of substrates reversible primary binding. The model corresponds to the observed kinetics of product accumulation withi
Publikováno v:
Biochemistry international. 17(3)
Transketolase from baker's yeast is rapidly inactivated in the presence of N-acetylimidazole. According to kinetic data, acetylation of one amino acid residue of the protein per active site is sufficient for TK* inactivation. The holoenzyme is inhibi