scholarly journals Adsorption and inactivation of proteolytic enzymes by Triaenophorus nodulosus (Cestoda)

2017 ◽  
Vol 54 (1) ◽  
pp. 3-10 ◽  
Author(s):  
G.I. Izvekova ◽  
T.V. Frolova ◽  
E.I. Izvekov
Keyword(s):  
Proteolytic Activity ◽  
Incubation Medium ◽  
Proteolytic Enzymes ◽  
Surrounding Medium ◽  
Serine Proteinases ◽  
Suppressive Activity ◽  
Triaenophorus Nodulosus

Summary The proteolytic activity in washings off the Triaenophorus nodulosus cestode tegument and the ability of the worms to inactivate proteolytic enzymes were studied. It was found that the major proteolytic activity in the washing samples is represented by the easily desorbed fraction most probably characterizing the activity of the host’s enzymes. Serine proteinases are an essential part of these enzymes. It was shown that the worms’ incubation medium and their homogenates can inhibit host proteinases and commercial trypsin samples. Suppressive activity of the incubation medium suggests that the inhibitors are rather spontaneously produced by the worms than induced by the presence of proteinases in the surrounding medium. The inhibitor produced by the cestode is hypothesized to be trypsin-specific.

scholarly journals The effect of melanin on the proteolytic potential of blood under alkali esophageal burn

2020 ◽  
Vol 93 (1) ◽  
Author(s):  
Nataliia Chornenka ◽  
Liudmyla Domylivska ◽  
Olga Kravchenko ◽  
Tetiana Koval ◽  
Liza Torgalo ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
Proteinase Inhibitors ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Serine Proteinases ◽  
Medical Problems ◽  
Α2 Macroglobulin ◽  
Old Rats ◽  
Hydrolysis Of ◽  
Esophageal Burn

Caustic esophageal burns are among serious medical problems of global significance. Due to a key role in biological processes proteolytic enzymes actively involved in the pathological mechanisms underpinning the development and progression of burn-related complications. Since melanin possesses a broad spectrum of biological activities we have investigated whether this compound can influence the proteolytic activity and level of proteinase inhibitors in the blood of rats with an alkali esophageal burn. Alkaline esophageal burns, which correspond to the first and second degree of burn, were induced by 10% and 20% NaOH, respectively. White, nonlinear, immature (4 weeks old) rats were used in the experiment. Total proteolytic activity was measured using casein as a substrate. The activities of α1- antitrypsin and α2-macroglobulin were measured considering the degree of inhibition of hydrolysis of N-benzoyl-L-arginineethyl ester. The fraction of serine proteinases was obtained by affinity chromatography on a benzamidine sepharose column. The qualitative composition of serine proteinases fraction was analyzed by zymography technique. According to the data obtained, the pathogenesis of alkaline esophageal burn is accompanied by a significant increase in the total proteolytic activity, activity of serine proteinases, and activity of α1-antitrypsin and α2-macroglobulin compared with the control rats. The present results clearly indicated that melanin is able to normalize the proteolytic homeostasis by affecting the activity of serine proteinases and the level of proteinase inhibitors in the plasma of rats with alkali esophageal burns.

scholarly journals Proteolytische Aktivität der lysosomalen Enzyme in der Leber wachsender Mäuse

2000 ◽  
Vol 43 (4) ◽  
pp. 363-374
Author(s):  
M. Schmidt ◽  
T. Król ◽  
U. Renne ◽  
L. Panicke
Keyword(s):  
Postnatal Development ◽  
Proteolytic Activity ◽  
Cathepsin D ◽  
Proteolytic Enzymes ◽  
Body Growth ◽  
Male Mice ◽  
High Body

Abstract. Title of the paper: Lysosomal proteolytic activity in the liver of growing mice The behaviour of the activity of some lysosomal proteolytic enzymes in Üie liver of mice, both selected and unselected for high body growth, was followed during the postnatal development. The activity of cathepsin D and L, the alanylaminopeptidase, the arginylaminopeptidase, the α-glucosidase and the N-acetyl-glucosaminidase was estimated in male mice aging 21, 28, 35 and 42 days. In the liver of animals with high body gain statistic significant lower activities (30–50 %) of all estimated enzymes were found, in comparison to the control mice. These results confirm the Statement mat inhibition of proteolysis is an immediate mechanism in the induction of growth.

scholarly journals Non-conventional affinity chromatography of serine proteinases and their inhibitors.

2003 ◽  
Vol 50 (3) ◽  
pp. 765-773 ◽  
Author(s):  
Antoni Polanowski ◽  
Anna Wilimowska-Pelc ◽  
Jolanta Kowalska ◽  
Joanna Grybel ◽  
Monika Zelazko ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Proteinase Inhibitor ◽  
Proteolytic Enzymes ◽  
Trypsin Inhibitors ◽  
General Description ◽  
Separation Procedure ◽  
Serine Proteinases ◽  
High Concentration ◽  
Porcine Pancreas ◽  
Nacl Concentration

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 alpha(1)-proteinase 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.

scholarly journals SELECTED PROTEOLYTIC ACTIVITY BY EXTRACTS OF DERMESTID LARVAE

2011 ◽  
Vol 19 (19) ◽  
pp. 79-83
Author(s):  
Lavinel G. IONESCU
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Proteolytic Activity ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
High Specific Activity ◽  
Water Extract ◽  
Dermestes Maculatus ◽  
Crude Preparation

The larvae of the Beetle Dermestes maculatus De Geer can subsist on a diet consisting largely of protein. Studies have been undertaken to investigate the nature of proteolytic enzymes. A water extract of the larvae yielded a crude preparation that hydrolyzes gelatin, bide powder, hemoglobin substrate, benzoyl-DL-arginine p-nitroamilide, and glutaryl-L-phenylalanine p-nitroanilide. Enzyme activity was found in a non-dialyzable, heat- and acid0labile portion of the extract yielded two fractions with high specific activity towards gelatin. These are precipitated between 40% to 60% saturation of ammonium sulfate and 60% to 80% saturation. The higher specific activity was observed in the 40%-60% fraction. These results suggest that the larvae of these dermestids contain proteolytic enzymes with actions similar to mammalian trypsin and chymotrypsin. The results also suggest that other proteolytic enzymes may be present as well.

Histological and Biochemical Observations of Developing Enameloid of the Sea Bream

1987 ◽  
Vol 1 (2) ◽  
pp. 191-195 ◽  
Author(s):  
K. Kawasaki ◽  
S. Shimoda ◽  
M. Fukae
Keyword(s):  
Proteolytic Activity ◽  
Developmental Stages ◽  
Proteolytic Enzymes ◽  
Sea Bream ◽  
Total Protein Content ◽  
Noncollagenous Proteins ◽  
Saturated Atmosphere ◽  
Tooth Germs ◽  
Water Saturated ◽  
Cryostat Sections

In order to study changes in the enameloid matrix of the Sea Bream during the course of its development, we selected the developmental tooth germs of this fish as representative of three different developmental stages: "chalk-like", "cheese-like", and "soft" enameloid. The protein, calcium, and phosphate contents of each sample were analyzed. The changes of the total protein content in each sample suggest that a major part of the proteins decreased during maturation, although newly formed enameloid of the Sea Bream contains collagen and noncollagenous proteins. The existence of proteolytic activity was examined by placement of undemineralized cryostat sections of unfixed tooth germs on exposed and processed photographic films and then incubation for 30 min in a water-saturated atmosphere at 37°C. Proteolytic activity could be detected in the enameloid matrix, which appeared to be in a "cheese-like" stage. It is suggested that proteolytic enzymes play an important role in the removal of proteins during the maturation of enameloid, although the detailed mechanism of the process is still obscure.

A study on the degradation of arachin by proteolytic enzymes

1973 ◽  
Vol 51 (11) ◽  
pp. 2217-2222 ◽  
Author(s):  
R. B. van Huystee
Keyword(s):  
Amino Acids ◽  
Proteolytic Activity ◽  
Free Amino Acids ◽  
Free Amino ◽  
Proteolytic Enzymes ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gels ◽  
Macromolecular Protein

The prime purpose of this proteolysis study was to direct attention to alternate means of measuring proteolytic activity other than the determination of free amino acids. The release of peptides from a macromolecular protein during incubation with either papain, pronase, or trypsin was determined by measuring the presence of 280-nm-absorbing molecules in the fractionation range of Sephadex G 25 eluant after incubation. The formation of larger proteinaceous constituents by proteolysis of arachin was analyzed by disc electrophoresis on polyacrylamide gels. Using these techniques it was noted that papain was the most efficient proteolytic agent for the degradation of arachin.

Mise en évidence d'une production de protéases exocellulaires par les levures au cours de la fermentation alcoolique du moût de raisin

OENO One ◽  
1980 ◽  
Vol 14 (1) ◽  
pp. 37 ◽  
Author(s):  
Michel Feuillat ◽  
G. Brillant ◽  
J. Rochard ◽  
Chantal Hory
Keyword(s):  
Nitrogen Content ◽  
Proteolytic Activity ◽  
Alcoholic Fermentation ◽  
Proteolytic Enzymes ◽  
Malolactic Fermentation ◽  
Soluble Nitrogen ◽  
Proteolytic Stability ◽  
Short Time

<p style="text-align: justify;">La durée d'activité très limitée dans le temps des protéases du raisin est confirmée en vinification en blanc, mais une nouvelle activité protéolytique peut être caractérisée à 37 °C et à pH 3,7 dans le moût au cours de la fermentation alcoolique.</p><p style="text-align: justify;">Cette activité doit être attribuée à des protéases exocellulaires libérées dans le milieu des levures. Parmi les souches essayées <em>S. bayanus</em> a une activité protéolytique plus importante que <em>S. cerevisiae</em>, ce qui se traduit par l'obtention de vins plus riches en azote soluble, donc plus stables du point de vue protéique et vraisemblablement d'une meilleure fermentescibilité malolactique.</p><p style="text-align: justify;">+++</p><p style="text-align: justify;">The short time of activity of grape proteolytic enzymes is confirmed in fermentation off skins. However, a new proteolytic activity has been characterized at 37 °C and at pH 3.7, occuring in alcoholic fermentation of the must.</p><p style="text-align: justify;">This activity comes from exocellular proteolytic enzymes released by the yeasts in the medium. Among tested strains <em>S. bayanus</em> has a proteolytic activity greater than <em>S. cerevisiae</em>; so the soluble nitrogen content of wines is higher. According to this, proteolytic stability is better as, probably, malolactic fermentation capabilities.</p>

Some characteristics of extracellular proteases produced by members of the Chytridiales and the Spizellomycetales (Chytridiomycetes)

1994 ◽  
Vol 40 (2) ◽  
pp. 106-112 ◽  
Author(s):  
Thomas Krarup ◽  
Lauritz W. Olson ◽  
Hans Peter Heldt-Hansen
Keyword(s):  
Proteolytic Activity ◽  
Isoelectric Focusing ◽  
Serine Proteases ◽  
Proteolytic Enzymes ◽  
Complex Compounds ◽  
Extracellular Proteases ◽  
Peptide Substrates ◽  
Proteolytic Activities ◽  
Selection Of

The extracellular proteolytic enzymes of eight saprophytic, eucarpic, and monocentric isolates from two genera of the order Spizellomycetales and from one genus of the order Chytridiales (Chytridiomycetes) have been partially characterized. The isolectric points of the proteases were estimated from zymograms and demonstrate the existence of three types of proteolytic activity in most isolates. The proteases were tested against synthetic chromogenic peptide substrates and a selection of cations and more complex compounds, and the results suggest that parts of the extracellular proteolytic activities are due to proteases from two groups: the Ca2+ stabilized proteases and the alkaline serine proteases.Key words: serine proteases, metalloproteases, Chytridiomycetes, isoelectric focusing, chromogenic peptide substrates.

Growth and proteinase production inPseudomonasspp. cultivated under various conditions of temperature and nutrition

1968 ◽  
Vol 35 (3) ◽  
pp. 385-393 ◽  
Author(s):  
H. S. Juffs ◽  
A. C. Hayward ◽  
H. W. Doelle
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Proteolytic Activity ◽  
Proteolytic Enzyme ◽  
Organic Nitrogen ◽  
Proteolytic Enzymes ◽  
Dry Weight ◽  
Growth Cycle ◽  
Logarithmic Phase ◽  
Proteinase Production

SummaryA study was made of the formation of the extracellular proteolytic enzymes during the growth cycle of several species ofPseudomonascultivated under different conditions of temperature and nutrition. Proteolytic activity was not proportional to growth. Expressed per unit of cell dry weight, the proteolytic activity showed a peak in the early logarithmic phase which was greater in cultures grown at 3 than at 28°C. Proteolytic enzyme was not formed in the absence of organic nitrogen. Of 16 organisms studied,Pseudomonas aeruginosaATCC 10145 was the most prolific producer of proteolytic enzyme.

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