Wyniki wyszukiwania - AGRO

1

Activation of latent human granulocyte gelatinase by rat mast cell protease

100%

Sopata I., Wojtecka-Lukasik E., Maslinski S.

Folia Histochemica et Cytobiologica

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1986

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tom 24

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nr 2

2

Senescence-dependent degradation of Lhcb3 polypeptide is mediated by thylakoid membrane-associated protease

100%

Zelisko A., Jackowski G.

Cellular and Molecular Biology Letters

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2002

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tom 07

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nr Suppl.

3

Optimization of bioinsecticides overproduction by Bacillus thuringiensis subsp. kurstaki using linear regression

86%

Ennouri K., Hassen H. B., Zouari N.

Polish Journal of Microbiology

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2013

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tom 62

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nr 3

A multiple linear regression analyses were performed to screen for the significant factors simultaneously influencing production of delta-endotoxin, proteolytic activities and spore formation by a Bacillus thuringiensis kurstaki strain. Investigated factors included: pH of the medium, available oxygen and inoculum size. It was observed that oxygen availability was the most influencing setting on both deltaendotoxins production and spores counts, followed by initial pH of the medium and inoculum size. On other hand, pH of medium was found to be the most significant parameter for proteolytic activity, followed by inoculum size and dissolved oxygen. Our results suggested that the first order with two-factor interaction model seemed to be more satisfactory than simple first order model for optimization of delta-endotoxin overproduction. The coefficients of determination (R²) indicated a better adequacy of the second order models to justify the obtained data. Based on results, relationships between delta-endotoxins production, proteolytic activities and spores counts were established. Our results can help to balance delta-endotoxins production and its stability.

4

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In silico studies of selected xanthophylls as potential candidates against SARS-CoV-2 targeting main protease (Mpro) and papain-like protease (PLpro)

86%

Karpinski T. M., Kwasniewski M., Ozarowski M., Alam R.

Herba Polonica

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2021

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tom 67

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nr 2

5

AtDeg2 - a chloroplast protein with dual protease/chaperone activity

86%

Jagodzik P., Adamiec M., Jackowski G.

Acta Societatis Botanicorum Poloniae

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2014

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tom 83

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nr 3

Chloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.

6

Serodiagnosis of Fasciola gigantica infection in buffaloes with native cathepsin-L proteases and recombinant cathepsin L1-D

86%

Aftab A., Lall R., Bisen S., Anandanarayanan A., Rialch A., Chamuah J. K., Yadav S., Silamparasan M., Raina O. K.

Acta Parasitologica

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2020

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tom 65

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nr 2

7

Transforming growth factor-beta activation in cell-free extracellular matrix preparations. Commentary

86%

Couchman J. R.

Folia Histochemica et Cytobiologica

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2019

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tom 57

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nr 4

8

Effect of physical and chemical factors in production of alkaline protease enzyme by Bacillus strains

86%

Tebyanian H., Mirhosseiny S. H., Bakhtiari A., Karami A., Dadseresht S., Otroshi B.

International Letters of Natural Sciences

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2018

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tom 71

Proteases is family of enzymes and it has crucial role due to their physiological roles and very valuable commercial applications. Alkaline protease are produced by Bacillus species are particular importance because of their thermal stability and stability at different pH values. This study aimed to investigate the effect of physical and chemical factors in production of alkaline protease enzyme fermentation by members of the genus Bacillus. In this study, alkaline protease enzyme production were evaluated in submerged fermentation by Bacillus strains which were isolated from alkaline soils of Guilan province. Factors incubation were optimized such as time, pH, amount of inoculation and ammonium sulfate in alkaline protease enzyme production whit using response surface methodology (RSM) in culture. The maximum enzymatic activity was observed in incubation time of 36 hours, pH=9, inoculation amount of 15% (V) and ammonium sulfate 1.5% (W/V). Factors had significant effect on the production of alkaline protease enzyme such as pH and ammonium sulfate.

9

Next-generation nutraceuticals: bioactive peptides from plant proteases

86%

Matkawala F., Nighojkar S., Nighojkar A.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2022

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tom 103

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nr 4

10

Use of yeast enzymes in degradation of paracasein curd

86%

Niedbalska J., Szoltysik M., Zelazko M., Dabrowska A., Chrzanowska J.

Polish Journal of Food and Nutrition Sciences

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2007

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tom 57

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nr 4[B]

11

Proteases and their inhibitors in the host-parasite system. XI. The activity of proteases of some mammalian organs after Ascaris tegument homogenate administration, and in experimental larval ascariasis

86%

Kadlubowski R., Wojcik A.

Acta Parasitologica

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1992

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tom 37

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nr 4

Subcutaneous injection of Ascaris lumbricoides suis homogenate in guinea pigs causes a significant increase of "neutral" spleen homogenate proteases, as well as of the activity of the splenic and renal post- nuclear fraction in days 2 or 3. Also, in experimental larval ascariasis in guinea pigs, a rise of proteolytic activity in the post-nuclear spleen fraction is observed 7 to 8 days after infection. The activity of "neutral" lung proteases in animals receiving Ascaris homogenate shows only tendency to increase. The proteolytic activity of liver, kidneys and heart preparations did not reveal significant differences in guinea pigs after Ascaris homogenate administration, nor in experimental larval ascariasis.

12

A comparison of methanol and ethanol effects on the activity and distribution of lysosomal proteases

86%

Skrzydlewska E., Roszkowska A., Moniuszko-Jakoniuk J.

Polish Journal of Environmental Studies

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1999

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tom 08

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nr 4

The activity of lysosomal proteolytic enzymes (cathepsin A, B, C, D and E) in cytosol and in the liver homogenate and in the blood plasma of rats intoxicated with methanol and ethanol was measured 6, 12 and 24 h and 2, 5 and 7 days after the intoxication. The activity of all proteases was increased in the cytosol from 12h to 5 days of alcohols intoxication, whereas the activity of these enzymes was decreased in the liver homogenate during the same time. Ethanol caused a higher increase in cytosol proteases activity than methanol. The magnitude of the decrease in proteolytic activity in the liver homogenate depends on the amino acid active center of the enzyme and on the kind of alcohol. The greatest decrease was observed for sulfhydryl and hydroxyl proteases and a smaller one for carboxyl proteases. Moreover methanol caused a greater decrease than ethanol. It was shown that the lysosomal proteases activity in the plasma was increased from 12 h to 5 days after alcohols intoxication and ethanol caused only a little less changes than methanol. The increase in the liver lipid peroxidation products examined as tiobarbituric acid reactive substances was also observed at the same time. These results indicate that during methanol and ethanol intoxication the cellular and lysosomal membranes are impaired and proteases are translocated into the blood. However, changes in proteases activities and proteases distribution within the hepatocytes may lead to disturbances in the catabolism of cell proteins and to destruction of liver cells.

13

Activity of liver proteases in experimental methanol intoxication

86%

Skrzydlewska E., Skrzydlewski Z., Worowski K.

Acta Biochimica Polonica

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1997

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tom 44

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nr 2

Intoxication of rats with methanol (1.5 and 3.0 g/kg body weight) led to a significant, time- and dose-dependent decrease in the activities of cathepsins A, B and C, while the activity of cathepsin D was unaffected. The decrease was associated with a different partial release of individual cathepsins to the post-lysosomal fraction.

14

Ocena podatności białek serwatkowych na działanie zewnątrzkomórkowych proteaz drożdży Yarrowia lipolytica

72%

Babij K., Dabrowska A., Szoltysik M., Pokora M., Szmyt A., Zambrowicz A., Chrzanowska J.

Acta Scientiarum Polonorum. Biotechnologia

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2013

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tom 12

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nr 3

Celem podjętych w pracy badań była ocena podatności wybranych białek serwatkowych na działanie zewnątrzkomórkowych proteaz drożdży Yarrowia lipolyti- ca i określenie ich potencjalnej przydatności technologicznej w procesie enzymatycznej hydrolizy. Do badań wykorzystano zarówno aktywną w środowisku kwaśnym proteazę aspartylową, a także działającą w środowisku alkalicznym proteazę serynową. Hydrolizie poddano a-laktoalbuminę, P-laktoglobulinę oraz dostępny w handlu koncentrat białek serwatkowych (WPC-80). Reakcję hydrolizy prowadzono w temperaturze 37°C, w pH 3,0 (dla proteazy aspartylowej) i w pH 8,0 (dla proteazy serynowej), wprowadzając enzym w dawce 10 U/mg białka substratowego. Postęp proteolizy analizowano ilościowo poprzez oznaczenie stopnia hydrolizy (DH%) i przyrost wolnych grup aminowych oraz jakościowo, tj. elektroforetycznie, a także wykonując rozdział frakcji białkowo-peptydowych przy wykorzystaniu wysoko sprawnej chromatografii cieczowej w układzie odwróconych faz (RP-HPLC). W puli wszystkich przetestowanych wariantów badawczych najwyższy poziom degradacji sięgający 39% uzyskano w roztworach P-laktoglobuliny trawionych drożdżową protezą serynową.

15

Factors affecting hydrolytic enzymes production by Yarrowia lipolytica strains

72%

Gdula A., Chrzanowska J., Szoltysik M., Kiezel X., Wojtatowicz M.

Acta Scientiarum Polonorum. Biotechnologia

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2002

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tom 01

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nr 1-2

16

Effect of carbon source on the production of lytic enzymes by filamentous fungi of the Trichoderma genus

72%

Piegza M., Szlaczka K., Laba W., Witkowska D.

Electronic Journal of Polish Agricultural Universities. Series: Biotechnology

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2014

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tom 17

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nr 2

17

New proteases of the chloroplast envelope – what do they do there?

72%

Adam Z.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 3

18

Keratinolytic potential of feather-degrading Bacillus polymyxa and Bacillus cereus

72%

Laba W., Rodziewicz A.

Polish Journal of Environmental Studies

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2010

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tom 19

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nr 2

371-378

Keratinolytic abilities of Bacillus polymyxa B20 and B. cereus B5esz were evaluated in liquid cultures in mineral media containing chicken feathers. Both tested strains were capable of effective liquefying and biodegradation of feather keratin, up to 56.5 – 72.1% in ten-day cultures, releasing considerable amounts of hydrolysis products. Tested bacteria were mesophilic species, producing highest activity of keratinases and proteases in the presence of keratin (1%) as a sole nutrient source or keratin supplemented with yeast extract, at 30℃. Keratinases of B. polymyxa were predominantly highly alkaline serine proteases, with optimum activity at 50℃, while B. cereus produced mainly a mixture of neutral proteases, optimally active at 45℃. Keratinolytic potential of tested bacterial strains could find a variety of applications, including utilization of keratinous waste from poultry industry and obtaining keratin hydrolysate-based soil fertilizers.

19

Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?

72%

Palesch D., Sienczyk M., Oleksyszyn J., Reich M., Wieczerzak E., Boehm B., Burster T.

Acta Biochimica Polonica

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2011

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tom 58

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nr 1

In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named α-protease and was active under neutral conditions. The second was named β-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical α-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The β-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.

20

Physiological and biochemical aspects of flower development and senescence in Nicotiana plumbaginifolia Viv.

72%

Nisar S., Tahir I., Ahmad S. S., Dar R. A.

Folia Horticulturae

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2017

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tom 29

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nr 1

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