Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Vladimír Leško"'
Autor:
Vladimír Leško
Publikováno v:
Ostium, Vol 13, Iss 2 (2017)
The philosophical work of Jan Patočka offers a unique intellectual synthesis of historical-philosophical and philosophical reflections on the basis of phenomenology. His philosophical message has become one of the most important ones within the phen
Externí odkaz:
https://doaj.org/article/247e1bda9dcd47dbbcdc3fc0faaf41e9
Autor:
Vladimír Leško
Publikováno v:
Filozofia. 76:364-376
Autor:
Vladimír Leško
Publikováno v:
Filozofia. 77:67-69
Autor:
Vladimír Leško
Publikováno v:
Idea. Studia nad strukturą i rozwojem pojęć filozoficznych. :63-74
Publikováno v:
Journal of the Serbian Chemical Society, Vol 75, Iss 2, Pp 185-194 (2010)
In this work, the binding of coenzymes to yeast alcohol dehydrogenase (EC 1.1.1.1) were investigated. The main criterions were the change in the standard free energies for individual reaction steps, the internal equilibrium constants and the overall
Externí odkaz:
https://doaj.org/article/d2e345225f6a421788f9b9d2062e38a0
Publikováno v:
Journal of the Serbian Chemical Society, Vol 73, Iss 4, Pp 393-403 (2008)
The survey of crystallographic data from the Protein Data Bank for 37 structures of trypsin and other serine proteases at a resolution of 0.78–1.28 Å revealed the presence of hydrogen bonds in the active site of the enzymes, which are formed betwe
Externí odkaz:
https://doaj.org/article/2e0239a6ef9542669b5c5aed2f7a54b6
Publikováno v:
Journal of the Serbian Chemical Society, Vol 68, Iss 2, Pp 77-84 (2003)
In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25°C, have been estimated. The determination of the individual rate constants was achieved by fitting
Externí odkaz:
https://doaj.org/article/fba00dda22cb4c46aab477caddfc80bb
Autor:
VLADIMIR LESKOVAC, SVETLANA TRIVIC
Publikováno v:
Journal of the Serbian Chemical Society, Vol 65, Iss 4, Pp 207-227 (2000)
1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10. Hydride transfer
Externí odkaz:
https://doaj.org/article/2fdcd7caf95d421784667fb863c1f410