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pro vyhledávání: '"G. V. Kolosova"'
Autor:
G. V. Kolosova
Publikováno v:
Sociology and Law. 15:79-87
The paper investigates the implementation of digital solutions and technologies in the social services for senior citizens in terms of the national project “Demography”. Current changes, according to the author’s position, form a new and proble
Autor:
I A, Grigoryeva, G V, Kolosova
Publikováno v:
Advances in gerontology = Uspekhi gerontologii. 34(6)
Modern society is becoming more and more complex, not only technologies are changing, but also its socio-age structure. For the first time, mankind found itself in a situation where there are more elderly people than young people, and it turned out t
Publikováno v:
Vestnik Voronežskogo Gosudarstvennogo Universiteta Inženernyh Tehnologij, Vol 0, Iss 3, Pp 114-117 (2013)
Developing of new technology of bakery products with consuming properties "Danko" using natural sweetener-tagatose.
Publikováno v:
Biokhimiia (Moscow, Russia). 47(5)
The trypsin inhibitor from Gleditsia triacanthos (L.) seeds was purified by affinity chromatography on a column with trypsin-Sepharose 4B. The isolated inhibitor is a single-chain protein with molecular weight of about 20 000. The inhibitor suppresse
Publikováno v:
Biokhimiia (Moscow, Russia). 47(12)
The chymotrypsin inhibitor was isolated from honey locust (Gleditsia triacanthos L.) by chromatography on trypsin- and chymotrypsin-Sepharose 4B and by gel filtration on Sephadex G-75. The inhibitor can inhibit chymotrypsin but has no effect on tryps
Publikováno v:
Biokhimiia (Moscow, Russia). 47(4)
The protein proteinase inhibitor from kidney bean (isoinhibitor, pI 4.3) is a double-headed inhibitor with independent reactive sites for trypsin and chymotrypsin. The reactive site of the inhibitor for trypsin is Lys (22)- Ser (23) in the sequense .
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 19(5)
Covalent immobilization of the pancreatic trypsin inhibitor onto a polymeric carrier was accomplished by introducing a double C = C bond in the inhibitor with a subsequent copolymerization of the activized inhibitor with acrylamide and N,N'-methylene