Wyniki wyszukiwania - AGRO

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Granulocyte proteinases as mediators of unspecific proteolysis in inflammation: a review

100%

Fritz H., Jochum M., Geiger R., Duswald K. H., Dittmer H., Kortmann S., Neumann S., Lang H.

Folia Histochemica et Cytobiologica

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1986

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tom 24

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nr 2

2

On the spatial organization of ubiquitin-dependent proteolysis in HeLa cells

100%

Wojcik C.

Folia Histochemica et Cytobiologica

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1997

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tom 35

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nr 2

3

Control of postharvest longevity of cut leaves of Nephrolepis exaltata (L.) Schott.

86%

Skutnik E., Rabiza-Swider J.

Annals of Warsaw Agricultural University. Horticulture and Landscape Architecture

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2005

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tom 26

4

Susceptibility of yeasts isolated from dairy products to cystatin

86%

Chrzanowska J., Krajewska E., Saleh J., Szoltysik M., Trziszka T.

Polish Journal of Natural Sciences. Supplement

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2004

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tom 02

23-29

5

Antioxidant activity of the peptide fraction from Parmigiano-Reggiano cheeses at different ageing times

86%

Bottesini C., Paolella S., Lambertini F., Galaverna G., Dossena A., Marchelli R., Sforza S.

Polish Journal of Food and Nutrition Sciences

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2011

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tom 61

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nr Suppl.1

6

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Biochemical and microbiological changes in cheese inoculated with Yarrowia lipolytica yeast

86%

Szoltysik M., Dabrowska A., Babij K., Pokora M., Zambrowicz A., Polomska X., Wojtatowicz M., Chrzanowska J.

Żywność Nauka Technologia Jakość

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2013

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tom 20

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nr 4

A Yarrowia lipolytica JII1c yeast strain, isolated from the Polish ‘Rokpol’ mould cheese, was used as an adjunct culture in the production of a Dutch-type cheese. Its effect on the microbiological and biochemical characteristics of the cheese was evaluated in this research study. Milk used to produce the cheese was inoculated with 105 cfu/mL yeast cells. During the ripening process, the yeast population grew systematically to reach a maximum level of 7.9 log cfu/g in the sixth week of maturation, whereas the number of lactic acid bacteria increased until the fourth week of ripening. Thereafter, the number of microorganisms in the both groups decreased. After 8 weeks of ripening, the pH value of cheese inoculated with yeasts was significantly higher than that of the control cheese sample (produced without those microorganisms) and reached the levels of 6.37 and 5.47, respectively. In the experimental cheeses, it was also found that the utilization rate of lactic and citric acids was higher. Additionally, the concentration levels of water-soluble nitrogen (WSN) and free amino groups (FAG) in the experimental cheeses were about twice as high as in the control cheese sample. A more intensive proteolysis in the experimental cheese was accompanied by a higher accumulation of biogenic amines, especially of tyramine, putrescine, and 2-phenylethylamine; in the experimental cheese, after 8 weeks, their contents amounted to: 167.01, 77.90, and 69.54 mg/100 g, respectively. In contrast, the concentration of histamine was similar in both cheeses (9.47 and 9.81 mg/100 g in the control and experimental cheese samples, respectively). Also, the experimental cheese revealed more pronounced lipolysis resulting in a higher accumulation of free fatty acids, especially of butyric, myristic, palmitic, stearic, and oleic acids. It can be concluded that the Y. lipolytica JII1c grew well in the cheese causing the ripening process of the cheese to significantly accelerate.

7

Structural insights into the regulation of SOS mutagenesis

86%

Gonzales M., Frank E. G., McDonald J. P., Levine A. S., Woodgate R.

Acta Biochimica Polonica

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1998

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tom 45

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nr 1

The Escherichia coli Umu proteins are best characterized by their role in damage inducible mutagenesis. Recently, we discovered that the intracellular levels of the UmuD and UmuC proteins are kept to a minimum by the Lon serine protease. Studies with the Salmonella typhimurium UmuD protein (which is 73% homologous with its E. coli counterpart) revealed that it too is degraded by Lon, suggesting that both UmuD proteins share conserved structural motifs. In contrast, E. coli UmuD' is removed from the cell by the ClpXP serine protease, but only when it is in a heterodimer complex with UmuD. We have generated deletion mutants of UmuD' and have co-expressed the mutant proteins with UmuD1 (a non-cleavable UmuD protein). By assaying the sensitivity of the mutant UmuD'-UmuD1 complex to ClpXP, we have been able to map regions of UmuD' that appear essential for efficient UmuD'-UmuD heterodimer formation. Previous experiments have suggested that the in vivo posttranslational processing of UmuD to UmuD' is inefficient. We have, however, discovered that limited cleavage occurs in an undamaged cell, but that these small amounts of UmuD' are rapidly degraded by ClpXP, thus giving rise to the appearance of inefficient cleavage. The ClpXP protease therefore plays dual roles in regulating SOS mutagenesis: it keeps the basal levels of UmuD' to a minimum in undamaged cells but it also acts in damaged cells to reduce the elevated levels of mutagenically active UmuD' protein, thereby returning the cell to a resting non-mutable state.

86%

Darewicz M., Mioduszewska H., Iwaniak A., Chojnowski W.

Natural Sciences

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1999

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tom 03

14

Influence of proteolitic proteasome activity inhibitors on Chara vulgaris spermiogenesis

86%

Kwiatkowska A., Wojtczak A., Poplonska K., Krupa A., Wlodarczyk J., Zabka A.

Acta Biologica Cracoviensia. Series Botanica. Supplement

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2000

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tom 42

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nr 1

15

Influences of pH on proteolysis in water solutions of milk protein concentrate and composition of rennet gels

86%

Zbikowska A., Szerszunowicz I.

Polish Journal of Natural Sciences

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2002

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tom 11

16

Modes of inhibition of cysteine proteases

86%

Rzychon M., Chmiel D., Stec-Niemczyk J.

Acta Biochimica Polonica

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2004

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tom 51

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nr 4

Cysteine proteases are involved in many physiological processes and their hyperactivity may lead to severe diseases. Nature has developed various strategies to protect cells and whole organisms against undesired proteolysis. One of them is the control of proteolytic activity by inhibition. This paper presents the mechanisms underlying the action of proteinaceous inhibitors of cysteine proteinases and covers propeptides binding backwards relative to the substrate or distorting the protease catalytic centre similarly to serpins, the p35 protein binding covalently to the enzyme, and cystatins that are exosite binding inhibitors. The paper also discusses tyropins and chagasins that, although unrelated to cystatins, inhibit cysteine proteinases by a similar mechanism, as well as inhibitors of the apoptosis protein family that bind in a direction opposite to that of the substrate, similarly to profragments. Special attention is given to staphostatins, a novel family of inhibitors acting in an unusual manner.

17

Development of a functional fermented peanut-based cheese analog using probiotic bacteria

72%

Sharma P., Sharma D., Amin A.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2018

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tom 99

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nr 4

18

Gonadoliberin (GnRH) and its copper complex (Cu-GnRH) enzymatic degradation in hypothalamic and pituitary tissue in vitro

72%

Herman A., Kozlowski H., Czauderna M., Kochman K., Kulon K., Gajewska A.

Journal of Physiology and Pharmacology

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2012

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tom 63

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nr 1

19

Immunoreactivity of chemically cross-linked gluten and hydrolysates of wheat flour

72%

Majak I., Leszczynska J., Lacka A.

Biotechnology and Food Science

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2011

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tom 75

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nr 2

20

Effect of chill storage time on proteolysis and lipid oxidation in vacuum-packed muscles from duck

72%

Przysiezna E.

Polish Journal of Food and Nutrition Sciences

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2007

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tom 57

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nr 4

457-463

Proteolysis and lipid oxidation in the vacuum-packed leg and breast muscles from Mullard drakes stored at 1°C were studied. As proteolysis indicators there were determined proteolytic activity, contents of amino nitrogen and free amino acids (FAA), and TBARS values as indicators of oxidative changes. Changes were also determined in the proteolytic activity, TBARS values and contents of: amino nitrogen and FAA. As a result, 18 FAA were found in breast muscles and 19 in leg and their total contents after 1 day of storage were 184.39 mg/100 g tissue, and 233.33 mg/100 g tissue (respectively). In the case of breast muscles a significant increase in the content of detected FAA (except Pro) was noted after 13 days of storage and in the leg muscles (except Asp) after 5 days of storage. It was established that the proteolytic activity decreased (ca. 38%) in breast after 18 days and in leg (ca. 30%) after 5 days of storage. The content of amino nitrogen significantly increased in breast muscles after 18 days and in leg muscles after 5 days of storage. During storage, TBARS values were observed to increase continuously in breast muscles, whereas in legs they first increased after 5 days and then were observed to decrease.

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