Wyniki wyszukiwania - AGRO

1

Some remarks on factors influencing on the effectiveness and specificity of the unlabeled peroxidase-antiperoxidase method in immunohistochemistry

100%

Kaluza J., Stachura J.

Folia Histochemica et Cytobiologica

|

1984

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tom 22

|

nr 3-4

2

Immunohistochemical evaluation of cathepsin D expression in colorectal cancer

100%

Chabowski A., Sulkowska M., Sulkowski S., Famulski W., Skrzydlewska E., Kisielewski W.

Folia Histochemica et Cytobiologica

|

2001

|

tom 39

|

nr 2

3

Airway remodeling in chronic obstructive pulmonary disease and asthma: the role of matrix metalloproteinase-9

86%

Grzela K., Litwiniuk M., Zagorska W., Grzela T.

Archivum Immunologiae et Therapiae Experimentalis

|

2016

|

tom 64

|

nr 1

4

Explant-like passaging of cells growing on portable substrata permits the avoidance of enzyme application and facilitates the passage procedure

86%

Ryszawy D., Podulka J., Tworzydlo A., Tomassy J., Jarmulski M., Madeja Z., Korohoda W.

Folia Biologica

|

2019

|

tom 67

|

nr 4

5

Genetic polymorphism of alpha-1-antitrypsin (Locus Pi) in Polish population determined by isoelectric focusing. I. Studies of Poznan and its region

86%

Kowalska A., Titenko N., Rujner J.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1991

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tom 39

|

nr 3

6

Emigration and accumulation of PMN-leukocytes induced by endotoxin, interleukin 1 and other chemotactic substances

86%

Movat H. Z., Cybulsky M. I., Golditz I. G.

Folia Histochemica et Cytobiologica

|

1986

|

tom 24

|

nr 2

7

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AtDeg2 - a chloroplast protein with dual protease/chaperone activity

86%

Jagodzik P., Adamiec M., Jackowski G.

Acta Societatis Botanicorum Poloniae

|

2014

|

tom 83

|

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.

8

Enhanced production, purification and characterization of alkaline keratinase from Streptomyces minutiscleroticus DNA38

86%

Allure N., D.N. M., Agsar D.

International Letters of Natural Sciences

|

2015

|

tom 43

A thermo tolerant, feather-degrading, newly isolated actinobacterial strain Streptomyces minutiscleroticus DNA38 was investigated for its ability to produce keratinase. Maximum production (283.4 IU) of keratinase by Streptomyces minutiscleroticus DNA38 in starch chicken feathers medium under submerged bioprocess was observed at optimized conditions of pH 9.0 of the medium and 45 °C incubation temperature. Further, an enhanced production (435.8 IU) of keratinase was achieved employing response surface methodology. Combined interactive effect of starch (7.50 g/L), yeast extract (0.74 g/L) and chicken feathers (7.50 g/L) were found to be the critical process variables for enhanced production under central composite design. Chicken feathers showed a direct action and addition of starch and yeast extract to the medium proved effective for a significant increase in the production of keratinase. The purified keratinase was monomeric and had a molecular mass of 29 kDa. The enzyme activity was significantly inhibited after pH 9.0 and temperature 50 °C.

9

Production of extracellular proteolytic enzymes by Beauveria bassiana

86%

Chrzanowska J., Kolaczkowska M.

Acta Mycologica

|

1998

|

tom 33

|

nr 2

10

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

|

2012

|

tom 63

|

nr 1

11

Differential glomerular immunoexpression of matrix metalloproteinases MMP-2 and MMP-9 in idiopathic IgA nephropathy and Schoenlein-Henoch nephritis

72%

Danilewicz M., Wagrowska-Danilewicz M.

Folia Histochemica et Cytobiologica

|

2010

|

tom 48

|

nr 1

63-67

12

Alkaline trypsin from the viscera and heads of Engraulis anchoita: partial purification and characterization

72%

Lamas D. L., Yeannes M. I., Massa A. E.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

|

2017

|

tom 98

|

nr 2

13

Wplyw roznych czynnikow na poziom aktywnosci aminopeptydazowej u bakterii Pseudomonas sp.

72%

Jankiewicz U., Sepowicz M., Sawicka D.

Acta Scientiarum Polonorum. Biotechnologia

|

2005

|

tom 04

|

nr 1-2

3-12

14

The influence of selected inhibitors on proteolytic enzymes activity in French bean

72%

Karas M., Baraniak B.

Electronic Journal of Polish Agricultural Universities. Series Food Science and Technology

|

2006

|

tom 09

|

nr 4

15

Extrachromosomal expression of nat05 gene encoding an alkaline serine protease from Bacillus subtilis N05

72%

Thu N. T. A., Chau N. T. T., Thien L. V., Huy N. D., Khue N. T. M., Hung N. B., Luong N. N., Thu L. T. A., Loc N. H.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

|

2018

|

tom 99

|

nr 4

16

The influence of isoprivet on neutrophil secretory action in the course of BRD in calves

72%

Wessely-Szponder J., Kloc K.

Electronic Journal of Polish Agricultural Universities. Series Veterinary Medicine

|

2010

|

tom 13

|

nr 4

17

Matrix metalloproteinases activity during the evolution of hypoxic-ischemic brain damage in the immature rat. The effect of 1-methylnicotinamide (MNA)

72%

Dragun P., Makarewicz D., Wojcik L., Ziemka-Nalecz M., Slomka M., Zalewska T.

Journal of Physiology and Pharmacology

|

2008

|

tom 59

|

nr 3

441-455

Matrix metalloproteinases (MMPs) are a family of proteolytic enzymes that degrade the extracellular matrix and carry out key functions during brain development. Apart from a physiological role, excessive activation of MMPs in brain tissue has been postulated to represent a pathway for cell death arising from ischemia. To evaluate the possible involvement of MMPs in the perinatal brain asphyxia, we exposed 7-day-old rats to hypoxia-ischemia (HI). Unilateral HI was administered by ligation of the common carotid artery followed by hypoxia (7.4% O2/92.6% N2) for 65 minutes. This insult is known to produce brain damage confined to the cerebral hemisphere ipsilateral to the arterial occlusion in > 90% of animals. HI resulted in a significant elevation of MMP-2 and MMP-9 activity in the ipsilateral forebrain. The maximum activation was found at 48 hours and 7-14 days after the insult. These results suggest that early and late induction of MMPs may play a role in neuronal death as well as in repair processes. The treatment of animals subjected to HI with 1-methylnicotinamide (MNA), the anti-inflammatory agent, led to the inhibition of MMP-9 in an acute phase of ischemic damage and to the activation of MMP-2 in the later stages after injury. The timing of MMPs modulation by MNA may indicate its possible therapeutic implications.

18

Cytochemical characterization of mucosubstances in the chick glandular stomach during embryonary and postnatal development

72%

Altamirano F., Avila R., Samar M. E., De Fabro S. P.

Folia Histochemica et Cytobiologica

|

1984

|

tom 22

|

nr 2

19

Expression of matrix metalloproteinase-9 in the neoplastic and interstitial inflammatory infiltrate cells in the different histopathological types of esophageal cancer

72%

Mroczko B., Kozlowski M., Groblewska M., Lukaszewicz M., Niklinski J., Laudanski J., Chyczewski L., Szmitkowski M.

Folia Histochemica et Cytobiologica

|

2008

|

tom 46

|

nr 4

471-477

20

Immobilisation of the proteolytic enzyme system [chymotrypsin-exopeptidases] in high-molecular polysaccharides

72%

Idziak J., Moszczynski P.

Polish Journal of Food and Nutrition Sciences

|

2000

|

tom 09/50

|

nr 1

Three kinds of high-molecular polysaccharides: alginate, chitosan and carrageenan, were tested as carriers for the immobilisation of proteolytic enzymes. The catalytic system consisted of the endopeptidase - chymotrypsin and exopeptidases: carboxypeptidase A and leucine aminopeptidase. Subsequently, this immobilised system was used for making of enzymatic hydrolysates of casein. In the case of periodic method of casein hydrolysis the best results (71.9% of tyrosine and tryptophan released) were achieved after 72 h, at substrate concentration 0.5% and with alginate as a carrier. In the semi-continuous method chitosan appeared to be the best carrier and after 72 h the degree of hydrolysis was 48.6% (52.7% of tyrosine and tryptophan released) at the concentration of casein 2%.

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