Wyniki wyszukiwania

1

Triphenylmethane dye as a substrate for chymotrypsin

100%

Kuczek M., Trojan C.

Acta Biochimica Polonica

|

1994

|

tom 41

|

nr 2

2

Serine proteinase inhibitors from insect hemolymph

88%

Polanowski A., Wilusz T.

Acta Biochimica Polonica

|

1996

|

tom 43

|

nr 3

Insect hemolymph, like vertebrate serum, contains several different types of polypeptides that are able to inhibit the catalytic function of proteolytic enzymes, however studies on proteins possessing this capability have been limited to a relatively few species. A comparative examination of the inhibition of trypsin, chymo- trypsin, neutrophil elastase and cathepsin G and pancreatic elastase by the hemolymph of 14 insect species belonging to six orders showed great diversity in terms of both total proteinase inhibitory capacity and specificity. Most of the inhibitors examined fall into two groups: low molecular mass proteins (below 10 kDa) related to Kunitz type inhibitors, and proteins of about 45 kDa which belong to the serpin superfamily of serine proteinase inhibitors. This minireview describes the properties, characteristics and possible biological significance of selected inhibitors.

3

Cathepsin A and chymotrypsin-like activity of the proteasome in human blood platelet

75%

Ostrowska H., Wojcik C., Worowski K.

Folia Histochemica et Cytobiologica

|

1999

|

tom 37

|

nr 2

4

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

The regulatory role of AtDeg5 chloroplast protease in chronological progression of principal growth stages in Arabidopsis thaliana plants

63%

Baranek M., Lucinski R., Jackowski G.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

|

2013

|

tom 94

|

nr 3

5

An inhibitor of the chymotrypsin-like activity of the proteasome [PSI] induces similar morphological changes in various cell lines

63%

Wojcik C.

Folia Histochemica et Cytobiologica

|

1997

|

tom 35

|

nr 4

6

Effect of different levels of cellulose in the diet on the proteolytic activity of the pancreas in broiler chickens

63%

Boguslawska-Tryk M.

Folia Biologica

|

2005

|

tom 53

|

nr Suppl.

7

Non-conventional affinity chromatography of serine proteinases and their inhibitors

63%

Polanowski A., Wilimowska-Pelc A., Kowalska J., Grybel J., Zelazko M., Wilusz T.

Acta Biochimica Polonica

|

2003

|

tom 50

|

nr 3

From among a wide variety of protein purification techniques affinity chromatography has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na+ but not K+ or Li+ ions are present in the reaction mixture. Taking advantage of this phenomenon the virgin forms of trypsin inhibitors from squash seeds, Kazal-type inhibitor from porcine pancreas and arproteinase inhibitor from human and sheep plasma, as an example, were separated using immobilized chymotrypsin or its inactive derivative methylchymotrypsin in the presence of 5 M NaCl.

8

Affinity purification of chicken pancreas proteinases and their N-terminal amino acid sequences

63%

Tluscik F., Polanowski A., Guyonnet V., Long P. L., Travis J.

Acta Biochimica Polonica

|

1994

|

tom 41

|

nr 2

9

Chymotryptic hydrolysis of lentil meal proteins and characteristics of the resulting hydrolysates

63%

Karamac M., Rybarczyk A.

Polish Journal of Food and Nutrition Sciences

|

2008

|

tom 58

|

nr 3

Lentil meal proteins were treated by chymotrypsin. Hydrolysis was controlled with the pH-stat method. Degree of hydrolysis (DH) was evaluated and after 120 min of the process amounted to 13%. SDS-PAGE and SE-HPLC methods were used to study molecular weight distribution of lentil meal proteins and their chymotryptic hydrolysates of DH 2%, 4%, 8% and 12%. Bands in the range of 21–66 kDa were predominant on the electrophoregram of lentil proteins. Chymotrypsin treatment resulted in releasing the hydrolysis products of both high molecular weight (62,000; 30,500 Da) molecules and small peptides (<6,500 Da). At the first stage of hydrolysis (DH 2.0%) intermediate products are formed, which are then further hydrolysed. Chromatographic separation confirmed the results of SDS-PAGE. Larger polypeptides and unhydrolysed proteins are present in hydrolysate of DH 12% but products of hydrolysis with molecular weight of 0.5–6.5 kDa are predominant. No simple correlation between degree of hydrolysis and intensity of bitterness and astringency sensation was noticed. Bitterness of hydrolysates was not high (2.25-2.35 a.u.).

10

Structural and functional diversities in lepidopteran serine proteases

63%

Srinivasan A., Giri A. P., Gupta V. S.

Cellular and Molecular Biology Letters

|

2006

|

tom 11

|

nr 1

Primary protein-digestion in Lepidopteran larvae relies on serine proteases like trypsin and chymotrypsin. Efforts toward the classification and characterization of digestive proteases have unraveled a considerable diversity in the specificity and mechanistic classes of gut proteases. Though the evolutionary significance of mutations that lead to structural diversity in serine proteases has been well characterized, detailing the resultant functional diversity has continually posed a challenge to researchers. Functional diversity can be correlated to the adaptation of insects to various host-plants as well as to exposure of insects to naturally occurring antagonistic biomolecules such as plant-derived protease inhibitors (PIs) and lectins. Current research is focused on deciphering the changes in protease specificities and activities arising from altered amino acids at the active site, specificity-determining pockets and other regions, which influence activity. Some insight has been gained through in silico modeling and simulation experiments, aided by the limited availability of characterized proteases. We examine the structurally and functionally diverse Lepidopteran serine proteases, and assess their influence on larval digestive processes and on overall insect physiology.

11

Inaktywacja roslinnych inhibitorow trypsyny i chymotrypsyny przez pepsyne

51%

Karwowska A., Gacko M., Guzowski A., Krupkowska A., Chojnacka-Zdrodowska A.

Bromatologia i Chemia Toksykologiczna

|

2005

|

tom 38

|

nr Supl.

349-351

Trawienie pepsyną ekstraktów nasion spożywanych przez człowieka powoduje obniżenie aktywności trypsyny i chymotrypsyny.

12

Effect of trypsin modulating oostatic factor (TMOF) on trypsin and chymotrypsin in Glyphodes pyloalis Walker (Lep.: Pyralidae) and Hyphantria cunea Drury (Lep.: Arctiidae)

51%

Ajamhassani M., Jalali Sendi J., Ghadamyary M., Borovsky D.

Pestycydy

|

2011

|

nr 1-4

In the present study, the effect of three concentrations of TMOF (7.5, 15 and 30 μg dissolved in water) on trypsin and chymotrypsin biosynthesis in 4th instar larvae of Glyphodes pyloalis walker and Hyphantria cunea Drury were studied 24 h and 48 h after injecting. Our results indicated that in G. pyloalis, lower concentrations (7.5 and 15 μg) inhibited trypsin biosynthesis at 24 h after injection. (P < 0.0001). TMOF, however, did not significantly affect trypsin biosynthesis at 48 h. In H. cunea, at 48 h after the injection, all concentrations (7.5, 15 and 30 μg per larvae) significantly inhibited trypsin biosynthesis (P < 0.05). Injections of TMOF did not significantly affect chymotrypsin in both insects. Although, in G. pyloalis, chymotrypsin activity decreased about 25% at 48 h after injection.

13

The effect of prostacyclin analogue-iloprost on the pancreas regeneration after cearulein-induced acute pancreatitis in rats

51%

Jurkowska G., Dlugosz J. W., Rydzewska G., Andrzejewska A.

Journal of Physiology and Pharmacology

|

1996

|

tom 47

|

nr 4

14

Activity of cuticle-degrading enzymes from entomopathogenic fungus Conidiobolus coronatus

51%

Czygier M., Samborski J., Dzik J. M., Walajtys-Rode E., Bogus M.

Wiadomości Parazytologiczne

|

1998

|

tom 44

|

nr 3

15

The directed enzymatic casein hydrolysis

51%

Idziak J., Moszczynski P.

Polish Journal of Food and Nutrition Sciences

|

1993

|

tom 02

|

nr 1

16

Proteinases of Streptomyces fradiae III. Catalytic and some physico-chemical properties of keratinolytic proteinase

51%

Galas E., Kaluzewska M.

Acta Microbiologica Polonica

|

1992

|

tom 41

|

nr 3-4

17

The influence of polyamines synthesis inhibition on pancreas regeneration and phospholipase D activity after acute caerulein induced pancreatitis in rats. Biochemical and ultrastructural study

51%

Jurkowska G., Rydzewska G., Andrzejewska A.

Journal of Physiology and Pharmacology

|

1997

|

tom 48

|

nr 4

18

Pancreatic regeneration after chronic ethanol feeding in rats

51%

Rydzewska G., Jurkowska G., Wroblewski E., Faszczewska A., Gabryelewicz A.

Journal of Physiology and Pharmacology

|

1999

|

tom 50

|

nr 2

19

NANC transmission in intestines and its pharmacological modulation

45%

Bauer V.

Acta Neurobiologiae Experimentalis

|

1993

|

tom 53

|

nr 1

20

Wplyw zwiazkow chemicznych wystepujacych w napojach alkoholowych na aktywnosc proteaz przewodu pokarmowego

38%

Gacko M., Worowska A., Roszkowska-Jakimiec W.

Bromatologia i Chemia Toksykologiczna

|

1996

|

tom 29

|

nr 1

71-77

Określano wpływ 26 napojów alkoholowych, ich destylatów i pozostałości podestylacyjnej na aktywność pepsynogenu, trypsynogenu i chymotrypsynogenu oraz aktywność pepsyny, trypsyny i chymotrypsyny.

Ograniczanie wyników

Triphenylmethane dye as a substrate for chymotrypsin

Serine proteinase inhibitors from insect hemolymph

Cathepsin A and chymotrypsin-like activity of the proteasome in human blood platelet

The regulatory role of AtDeg5 chloroplast protease in chronological progression of principal growth stages in Arabidopsis thaliana plants

An inhibitor of the chymotrypsin-like activity of the proteasome [PSI] induces similar morphological changes in various cell lines

Effect of different levels of cellulose in the diet on the proteolytic activity of the pancreas in broiler chickens

Non-conventional affinity chromatography of serine proteinases and their inhibitors

Affinity purification of chicken pancreas proteinases and their N-terminal amino acid sequences

Chymotryptic hydrolysis of lentil meal proteins and characteristics of the resulting hydrolysates

Structural and functional diversities in lepidopteran serine proteases

Inaktywacja roslinnych inhibitorow trypsyny i chymotrypsyny przez pepsyne

Effect of trypsin modulating oostatic factor (TMOF) on trypsin and chymotrypsin in Glyphodes pyloalis Walker (Lep.: Pyralidae) and Hyphantria cunea Drury (Lep.: Arctiidae)

The effect of prostacyclin analogue-iloprost on the pancreas regeneration after cearulein-induced acute pancreatitis in rats

Activity of cuticle-degrading enzymes from entomopathogenic fungus Conidiobolus coronatus

The directed enzymatic casein hydrolysis

Proteinases of Streptomyces fradiae III. Catalytic and some physico-chemical properties of keratinolytic proteinase

The influence of polyamines synthesis inhibition on pancreas regeneration and phospholipase D activity after acute caerulein induced pancreatitis in rats. Biochemical and ultrastructural study

Pancreatic regeneration after chronic ethanol feeding in rats

NANC transmission in intestines and its pharmacological modulation

Wplyw zwiazkow chemicznych wystepujacych w napojach alkoholowych na aktywnosc proteaz przewodu pokarmowego