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1.


   
    Green flavoprotein from P. leiognathi: purification, characterization and identification as the product of the lux G(N) gene / A. A. Raibekas // Journal of bioluminescence and chemiluminescence. - 1991. - Vol. 6, Is. 3. - P. 169-176 . - ISSN 0884-3996
Кл.слова (ненормированные):
bacterial protein -- flavoprotein -- amino acid sequence -- article -- bacterial gene -- chemistry -- genetics -- isolation and purification -- luminescence -- molecular genetics -- molecular weight -- Photobacterium -- Amino Acid Sequence -- Bacterial Proteins -- Flavoproteins -- Genes, Bacterial -- Luminescence -- Molecular Sequence Data -- Molecular Weight -- Photobacterium -- Support, U.S. Gov't, P.H.S.
Аннотация: A green flavoprotein (GFP) was isolated and purified to homogeneity from Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54,000 and contains two molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.

Scopus
Держатели документа:
Institute of Biophysics, USSR Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Raibekas, A.A.

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2.


   
    Inhibition effect of food preservatives on endoproteinases / E. N. Esimbekova [et al.] // Food Chem. - 2017. - Vol. 235. - P294-297, DOI 10.1016/j.foodchem.2017.05.059 . - ISSN 0308-8146
Кл.слова (ненормированные):
Endoproteinases -- Food additives -- Pancreatic disease -- Pancreatic enzymes -- Benzoic acid -- Enzyme activity -- Enzymes -- Food additives -- Food preservatives -- Potassium sorbate -- Sodium -- Acceptable daily intakes -- Decay constants -- Endoproteinases -- Human metabolisms -- Inhibition effect -- Light intensity -- Protein digestion -- Sodium benzoate -- Sorbic acid
Аннотация: The present manuscript proposes a novel approach to assess the impact of food additives on human metabolism by analysing their effect on biomarker enzyme activity. Alterations in the activity of pancreatic enzymes, such as chymotrypsin and trypsin, which are affected by the most common food preservatives, sodium benzoate (E211), potassium sorbate (E202) and sorbic acid (E200), have been evaluated. The proteinase activity was analysed with a bioluminescent method using the light intensity decay constant. Our study revealed that the preservatives reduce proteinase activity by 50% (EC50) at a much lower concentration than their acceptable daily intake (ADI). Thus, sodium benzoate and sorbic acid have an inhibition effect on chymotrypsin at concentrations 14 times lower and 70 times lower than their ADI and this increases with exposure time. Food preservative consumption impacts negatively on protein digestion, which is especially dangerous for patients with pancreatitis. © 2017 Elsevier Ltd

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation
Siberian Federal University, Institute of Fundamental Biology and Biotechnology, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Institute of Agro-ecological Technologies, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Esimbekova, E. N.; Asanova, A. A.; Deeva, A. A.; Kratasyuk, V. A.

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3.


   
    The use of bioluminescent biotests for study of natural and laboratory aquatic ecosystems / V. A. Kratasyuk [et al.] // Chemosphere. - 2001. - Vol. 42, Is. 8. - P909-915, DOI 10.1016/S0045-6535(00)00177-6 . - ISSN 0045-6535
Кл.слова (ненормированные):
Alcohol dehydrogenase -- Bacterial luciferase -- Bioluminescence -- Blooming -- Pollution -- Trypsin -- Water toxicity -- alcohol dehydrogenase -- benzoquinone -- luciferase -- trypsin -- aquatic ecosystem -- bioluminescence -- water quality -- article -- bacterium culture -- bioluminescence -- blue green alga -- ecosystem -- pond -- seasonal variation -- water pollution -- water quality -- Benzoquinones -- Biological Assay -- Cyanobacteria -- Ecosystem -- Environmental Monitoring -- Eutrophication -- FMN Reductase -- Indicators and Reagents -- Luminescent Measurements -- NADH, NADPH Oxidoreductases -- Water Pollutants -- Russian Federation -- algae -- Bacteria (microorganisms) -- Chlorophyta -- Cyanobacteria -- uncultured cyanobacterium
Аннотация: A set of bioluminescent tests was developed to monitor water quality in natural and laboratory ecosystems. It consisted of four bioluminescent systems: luminous bacteria, coupled enzyme system NADH:FMN-oxidoreductase-luciferase and triplet enzyme systems with alcohol dehydrogenase and trypsin. The set of biotests was applied for a small forest pond (Siberia, Russia), laboratory microecosystems polluted with benzoquinone and a batch culture of blue-green algae. Thereby effects of natural water compared to those of models of heavy pollution and "bloom" of blue-greens on the bioluminescent tests were revealed. The set of biotests was not affected by a natural seasonal variability of water quality in the unpolluted pond, but responded to the heavy pollution and the "bloom" of blue-greens. The set of biotests could be recommended as the alarm test to control the acute toxicity of natural water bodies. В© 2001 Elsevier Science Ltd.

Scopus
Держатели документа:
Krasnoyarsk State University, pr. Svobodnii 79, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Mira av., 88, Krasnoyarsk, 660049, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Esimbekova, E.N.; Gladyshev, M.I.; Khromichek, E.B.; Kuznetsov, A.M.; Ivanova, E.A.

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4.
А.с. 1027615 СССР, МКИ G 01 N 33/48.

   
    Способ определения активности протеаз [Текст] / В. Н. Петушков [и др.] ; Ин-т физ. им. Л. В. Киренского. - № 3311598/28-13 ; Заявл. 30.06.19811983. -
ГРНТИ
РУБ 343.15.19
Рубрики:
ПРОТЕАЗЫ
   ТРИПСИН КФ 3

   1

   АКТИВНОСТЬ

   ОПРЕДЕЛЕНИЕ

   МЕТОД

   БИОЛЮМИНЕСЦЕНЦИЯ

   NADH:FMN-ОКСИДОРЕДУКТАЗА КФ 1

   ЛЮЦИФЕРАЗА

   ПРИМЕНЕНИЕ

   ФЕРМЕНТНАЯ КОМПОЗИЦИЯ

   TRYPSIN EC

   ACTIVITY DETERMINATION

: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Петушков, Валентин Николаевич; Кратасюк, Г. А.; Фиш, А. М.; Гительзон, Иосиф Исаевич; Ин-т физ. им. Л. В. Киренского
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