scholarly journals Effect of different protein sources on protease activity of northern pike, Esox lucius Linneaus 1758, juvenile

2020 ◽  
Vol 37 (2) ◽  
pp. 135-138
Author(s):  
Cemil Kaya GÖKÇEK ◽  
Tamás SZABÓ ◽  
Cüneyt SUZER
Keyword(s):  
Proteolytic Activity ◽  
Protease Activity ◽  
Fish Meal ◽  
Soybean Protein ◽  
Northern Pike ◽  
Inhibitory Effect ◽  
Live Prey ◽  
Protein Sources ◽  
Corn Gluten

The aim of the study is to determine the inhibitory effect of different protein sources on protease activity of Northern pike, E. Lucius, during larval ontogeny. For this purpose, Northern pike were fed from yolk sac absorption until 21 days after hatching (DAH). At that point, larvae were sampled on 7, 14 and 21 DAH days and the activity of enzyme was analyzed in vitro. In the study, two different fish meal, chicken meal, krill meal, corn gluten, soybean protein concentrate, soybean meal and dried distillers grains with solubles were tested. Fish meal-I showed the lowest effect (7.53 %) on 7 DAH larvae. Moreover, chicken meal has the highest inhibitory effect on the proteases in the first week (68.27%). In the following period (DAH 14), although the inhibition ratio dramatically increased in all ingredients, fish meal-I has still the lowest effect on proteolytic activity (55.66%). In the same period, the highest effect was obtained from krill (82.28 %) and chicken meals (86.73 %), respectively. Then, there was no statistical difference between fish meal-I, fish meal-II and corn gluten in the 21 DAH and relatively lower than the others (p>0.05). Additionally, chicken meal again has the highest effect on juveniles with the ratio 89.27 %. As a result, the increase of proteolytic activity was notably increased in 7-14-21 DAH, however, it is concluded that feeding larvae and juveniles with live prey is still suggested to get better result for such a carnivorous species culture.

scholarly journals FURTHER STUDIES ON THE ROLE OF PROTEASES IN THE ALLERGIC REACTION

1961 ◽  
Vol 113 (2) ◽  
pp. 359-380 ◽  
Author(s):  
Georges Ungar ◽  
Takuso Yamura ◽  
Jacqueline B. Isola ◽  
Sidney Kobrin
Keyword(s):  
Amino Acid ◽  
Guinea Pig ◽  
Proteolytic Activity ◽  
Guinea Pigs ◽  
Protease Activity ◽  
Amino Acid Esters ◽  
Protein Substrates ◽  
Protease Activation ◽  
Acid Esters

Protease activity was measured through the hydrolysis of synthetic amino acid esters in body fluids and tissues of guinea pigs, rats, mice, and humans. Significant in vitro activation was observed in serum and lung slices of sensitized guinea pigs on addition of the specific antigen. Increased proteolytic activity was also seen in reverse anaphylaxis. More marked activation occurred when guinea pig serum was treated with peptone and guinea pig or rat serum was treated with agar. Protease activation was demonstrated in specimens of human skin under the influence of a poison ivy extract or croton oil added in vitro. Urinary protease activity of guinea pigs increased significantly during the first hours of anaphylactic shock and very markedly in peptone shock. Peptone shock, elicited in mice pretreated with H. pertussis, was accompanied by a considerable increase in protease activity in the peritoneal fluid as compared with non-pretreated mice which were insensitive to peptone. Proteolytic activity resulting from the activation procedures was due to a number of proteases. The dominant substrate affinity and inhibition patterns suggest that serum and urine proteases are similar to but not identical with plasmin. Anaphylactic activation exhibited patterns different from those resulting from the action of anaphylactoid agents. Tissue enzymes are either of cathepsin- or chymotrypsin-type or mixtures of both. Some of the activated enzymes, although remarkably effective in hydrolyzing amino acid esters, show no activity on protein substrates. This does not justify, however, their designation as "esterases." They probably belong to the class of specific proteases acting only on a single or a small number of functionally significant protein substrates. There is at present sufficient evidence to prove not only that protease activation does occur in anaphylaxis and anaphylactoid conditions but also that it is an important component of the chain of reactions leading to the allergic response.

scholarly journals The Serine Protease HhoA from Synechocystis sp. Strain PCC 6803: Substrate Specificity and Formation of a Hexameric Complex Are Regulated by the PDZ Domain

2007 ◽  
Vol 189 (18) ◽  
pp. 6611-6618 ◽  
Author(s):  
Pitter F. Huesgen ◽  
Philipp Scholz ◽  
Iwona Adamska
Keyword(s):  
Membrane Proteins ◽  
Substrate Specificity ◽  
Proteolytic Activity ◽  
Protease Activity ◽  
Elevated Temperatures ◽  
Critical Role ◽  
Pdz Domain ◽  
General Role ◽  
Pcc 6803

ABSTRACT Enzymes of the ATP-independent Deg serine endopeptidase family are very flexible with regard to their substrate specificity. Some family members cleave only one substrate, while others act as general proteases on unfolded substrates. The proteolytic activity of Deg proteases is regulated by PDZ protein interaction domains. Here we characterized the HhoA protease from Synechocystis sp. strain PCC 6803 in vitro using several recombinant protein constructs. The proteolytic activity of HhoA was found to increase with temperature and basic pH and was stimulated by the addition of Mg2+ or Ca2+. We found that the single PDZ domain of HhoA played a critical role in regulating protease activity and in the assembly of a hexameric complex. Deletion of the PDZ domain strongly reduced proteolysis of a sterically challenging resorufin-labeled casein substrate, but unlabeled β-casein was still degraded. Reconstitution of the purified HhoA with total membrane proteins isolated from Synechocystis sp. wild-type strain PCC 6803 and a ΔhhoA mutant resulted in specific degradation of selected proteins at elevated temperatures. We concluded that a single PDZ domain of HhoA plays a critical role in defining the protease activity and oligomerization state, combining the functions that are attributed to two PDZ domains in the homologous DegP protease from Escherichia coli. Based on this first enzymatic study of a Deg protease from cyanobacteria, we propose a general role for HhoA in the quality control of extracytoplasmic proteins, including membrane proteins, in Synechocystis sp. strain PCC 6803.

scholarly journals REPLACEMENT OF FISH MEAL PROTEIN BY SOY BEAN AND CORN GLUTEN MEAL PROTEINS IN THE DIET OF MUD CRAB, Scylla paramamosain

2009 ◽  
Vol 4 (1) ◽  
pp. 75
Author(s):  
Ketut Suwirya ◽  
Nyoman Adiasmara Giri ◽  
Muhamad Marzuqi
Keyword(s):  
Fish Meal ◽  
Scylla Paramamosain ◽  
Mud Crab ◽  
Corn Gluten Meal ◽  
Gluten Proteins ◽  
Protein Sources ◽  
Alternative Protein ◽  
Trash Fish ◽  
Corn Gluten ◽  
Meal Protein

Mud crab culture relies heavily on trash fish as the main source of feed ingredients. Artificial diets have been developed for mud crab and most of them have high content of fish meal. The increasing cost and demand of fish meal has encouraged feed manufacture to search for cheaper alternative protein sources such as plant protein. There is an urgent need to find suitable alternative protein sources to reduce the dependence of fish meal in mud crab diet. The objective of this study was to develop compounded feeds for juvenile of mud crab with reduced fish meal content, and as an alternative of trash fish feeding. For that reason, the experiment was done. Experimental diets were fish meal, 20% of soy bean (20% SBP), 40% of soy bean (40% SBP), 20% of corn gluten (20% CGP), and 40% of corn gluten meal protein (40% CGP). Average initial mud crab body weight of 0.65 ± 0.03 g was fed experimental diets for 56 days. The result showed that dietary fish meal protein can be replaced by 20% of soy bean and 20%–40% of corn gluten proteins for mud crab (Scylla paramamosain) diet. Thus, it can arguably be concluded that soy bean and corn gluten proteins are the alternative protein sources to partially replaced fish meal.

In Vitro Studies on a Proteolytic Enzyme from Aspergillus Oryzae (Protease I)

1968 ◽  
Vol 19 (01/02) ◽  
pp. 136-144 ◽  
Author(s):  
D Ogston ◽  
C. M Ogston
Keyword(s):  
Proteolytic Activity ◽  
Fibrinolytic Activity ◽  
Proteolytic Enzyme ◽  
Thrombolytic Agent ◽  
Inhibitory Effect ◽  
In Vitro Studies ◽  
Clotting Time ◽  
Proteolytic Action ◽  
Fibrinolytic Action

Summary1. Protease I was found to have potent fibrinolytic activity in concentrations which exceeded the blood inhibitory capacity when tested on fibrin plates and artificial thrombi.2. Plasma inhibited the proteolytic activity of protease I to a greater extent than serum; serum had a greater inhibitory effect on protease I than on plasmin. Trasylol did not inhibit the proteolytic action of protease I.3. Protease I caused the slow formation of fibrin in plasma in concentrations which did not produce fibrinogenolysis; this effect was seen in Al(OH)3-adsorbed plasma, and was not inhibited by heparin. Protease I also shortened the recalcified plasma clotting time.4. The fibrinogenolytic action of protease I was more rapid than its fibrinolytic action both in the presence and absence of plasma inhibitors. No concentration of protease I lysed fibrin in plasma without prior destruction or conversion to fibrin of the surrounding plasma fibrinogen.5. It is concluded from these in vitro studies that protease I does not have the properties necessary for a satisfactory thrombolytic agent.

scholarly journals Polyphenols from Chilean Propolis and Pinocembrin Reduce MMP-9 Gene Expression and Activity in Activated Macrophages

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Nicolás Saavedra ◽  
Alejandro Cuevas ◽  
Marcela F. Cavalcante ◽  
Felipe A. Dörr ◽  
Kathleen Saavedra ◽  
...  
Keyword(s):  
Gene Expression ◽  
Proteolytic Activity ◽  
Ethanolic Extract ◽  
Inhibitory Effect ◽  
Ethanol Solution ◽  
Dependent Manner ◽  
Propolis Extract ◽  
Joint Contribution ◽  
Ethanolic Extract Of Propolis

Polyphenols from diverse sources have shown anti-inflammatory activity. In the context of atherosclerosis, macrophages play important roles including matrix metalloproteinases synthesis involved in degradation of matrix extracellular components affecting the atherosclerotic plaque stability. We prepared a propolis extract and pinocembrin in ethanol solution. Propolis extract was chemically characterized using LC-MS. The effect of treatments on gene expression and proteolytic activity was measuredin vitrousing murine macrophages activated with LPS. Cellular toxicity associated with both treatments and the vehicle was determined using MTT and apoptosis/necrosis detection assays. MMP-9 gene expression and proteolytic activity were measured using qPCR and zymography, respectively. Thirty-two compounds were identified in the propolis extract, including pinocembrin among its major components. Treatment with either ethanolic extract of propolis or pinocembrin inhibits MMP-9 gene expression in a dose-dependent manner. Similarly, an inhibitory effect was observed in proteolytic activity. However, the effect showed by ethanolic extract of propolis was higher than the effect of pinocembrin, suggesting that MMP-9 inhibition results from a joint contribution between the components of the extract. These data suggest a potential role of polyphenols from Chilean propolis in the control of extracellular matrix degradation in atherosclerotic plaques.

scholarly journals The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83

2004 ◽  
Vol 72 (10) ◽  
pp. 5555-5564 ◽  
Author(s):  
Elaine Vanterpool ◽  
Francis Roy ◽  
Hansel M. Fletcher
Keyword(s):  
Proteolytic Activity ◽  
Porphyromonas Gingivalis ◽  
Protease Activity ◽  
Catalytic Domain ◽  
Immunoblot Analysis ◽  
Extracellular Protein ◽  
Transcriptional Unit ◽  
Wild Type ◽  
Defective Mutant

ABSTRACT Regulation/activation of the Porphyromonas gingivalis gingipains is poorly understood. A unique 1.3-kb open reading frame downstream of the bcp-recA-vimA transcriptional unit was cloned, insertionally inactivated with the ermF-ermAM antibiotic resistance cassette, and used to create a defective mutant by allelic exchange. In contrast to the wild-type W83 strain, the growth rate of the mutant strain (designated FLL93) was reduced, and when plated on Brucella blood agar it was nonpigmented and nonhemolytic. Arginine- and lysine-specific gingipain activities were reduced by approximately 90 and 85%, respectively, relative to activities of the parent strain. These activities were unaffected by the culture's growth phase, in contrast to the vimA-defective mutant P. gingivalis FLL92, which has increased proteolytic activity in stationary phase. Expression of the rgpA, rgpB, and kgp gingipain genes was unaltered in P. gingivalis FLL93 compared to that of the wild-type strain. Further, in extracellular protein fractions a 64-kDa band was identified that was immunoreactive with the RgpB-specific proenzyme antibodies. Active-site labeling with dansyl-glutamyl-glycyl-arginyl chloromethyl ketone or immunoblot analysis showed no detectable protein band representing the gingipain catalytic domain. In vitro protease activity could be slightly induced by a urea denaturation-renaturation cycle in an extracellular protein fraction, in contrast to the vimA-defective mutant P. gingivalis FLL92. Expression of flanking genes, including recA, vimA, and Pg0792, was unaltered by the mutation. Taken together, these results suggest that the vimA downstream gene, designated vimE (for virulence-modulating gene E), is involved in the regulation of protease activity in P. gingivalis.

scholarly journals Profile of the body surface proteolytic systém in Apis mellifera quee

2011 ◽  
Vol 56 (No. 1) ◽  
pp. 15-22 ◽  
Author(s):  
A.J. Strachecka ◽  
M.M. Gryzińska ◽  
M. Krauze ◽  
K. Grzywnowicz
Keyword(s):  
Protease Inhibitor ◽  
Honey Bee ◽  
Proteolytic Activity ◽  
Body Surface ◽  
Protease Activity ◽  
Serine Proteases ◽  
Developmental Stages ◽  
Cysteine Proteases ◽  
The Body

The proteolytic system on the body surface of the honey bee has been insufficiently researched. In this study the body surface proteolytic activity was examined in queens at various developmental stages (eggs, larvae, pupae and imagines) in different seasons (spring, summer, autumn, winter). Extracts of the body surface material with water and detergent were used for an in vitro analysis of the proteolytic activity and protease inhibitor level assaying, as well as for an electrophoretic separation of the extracts in polyacrylamide gels. The following methods were used: protein content testing by the Lowry method (modified by Schacterle-Pollack), protease activity testing by the Anson method and protease inhibitor activity testing by the Lee and Lin method. Our studies revealed a high protease activity in an acidic environment (pH = 2.4; the material rinsed with detergent), as well as in neutral (pH = 7) and alkaline (pH = 11.2) environments (the material rinsed with water in both cases). The highest protein concentration values were observed in the imagines from summer. The lowest activities of the proteases and protease inhibitors were determined in the eggs from summer. The highest activities of the acidic, neutral and alkaline proteases were observed in the pupae from spring. The highest number of protease activity bands in PAGE zymography was obtained for the neutral and alkaline activities in the queens for all the seasons. In the queens all the catalytic protease types were present: asparagine and cysteine proteases at pH = 2.4; cysteine proteases and metalloproteases at pH = 7 and serine proteases at pH = 11.2. These results were crucial for the analysis of immunity mechanisms on the body surface of the honey bee.

scholarly journals Impact of replacing fish meal by a mixture of different plant protein sources on the growth performance in Nile Tilapia (Oreochromis niloticus L.) diets

2017 ◽  
Vol 78 (3) ◽  
pp. 525-534 ◽  
Author(s):  
A. Al-Thobaiti ◽  
K. Al-Ghanim ◽  
Z. Ahmed ◽  
E. M. Suliman ◽  
S. Mahboob
Keyword(s):  
Growth Performance ◽  
Oreochromis Niloticus ◽  
Fish Meal ◽  
Wheat Gluten ◽  
Plant Protein ◽  
Corn Gluten Meal ◽  
Protein Sources ◽  
Plant Protein Sources ◽  
Corn Gluten ◽  
Plant Sources

Abstract The present study aimed to assess the appropriate level of replacement of fish meal (FM) with alternative plant sources in the feed fed to Oreochromis niloticus to evaluate the growth performance. Three isoproteinious (40% crude protein) diets were prepared from different ingredients viz., fish meal, corn gluten meal, wheat gluten meal, and bagasse kenna meal. O. niloticus showed a maximum increase in weight as 9.70, 11.09, 8.53 and 8.32 g during the 2nd, 2nd, 3rd and 2nd fortnight with feeding treatment A, B, C and D, respectively. The growth performance of the fish in terms of weight gain, specific growth rate, feed conversion ratio and protein efficiency ratio were found to be significantly (P < 0.05) higher in the fish fed with 20% replacement of fishmeal in diet B. The worst growth performance was observed in fish fed with commercial diet, designated as diet D. It was concluded that the fish meal can be replaced up to 20 percent with other plant protein sources without any negative impact on fish health. The replacement of fish meal with local plant sources (corn gluten meal, wheat gluten meal, soybean meal and bagasse kenna mix) will not only be beneficial to achieve better growth performance in O. niloticus, it will be a value addition as well.

The Effect of Ciprofloxacin on Tendon, Paratenon, and Capsular Fibroblast Metabolism

2000 ◽  
Vol 28 (3) ◽  
pp. 364-369 ◽  
Author(s):  
Riley J. Williams ◽  
Erik Attia ◽  
Thomas L. Wickiewicz ◽  
Jo A. Hannafin
Keyword(s):  
Cell Proliferation ◽  
Achilles Tendon ◽  
Protease Activity ◽  
Collagen Synthesis ◽  
Culture Media ◽  
Fibroblast Cell ◽  
Inhibitory Effect ◽  
Proteoglycan Synthesis ◽  
Ground Substance

The pathologic mechanisms underlying fluoroquinolone-induced tendinopathy are poorly understood. The observed incidence of tendinitis and tendon rupture in patients treated with ciprofloxacin hydrochloride suggests that the fluoroquinolone antibiotics alter tendon fibroblast metabolism. The purpose of this study was to examine the effect of ciprofloxacin on fibroblast metabolism in vitro. Canine Achilles tendon, paratenon, and shoulder capsule specimens were maintained in culture with ciprofloxacin (5, 10, or 50 g/ml). Fibroblast proliferation, collagen synthesis, proteoglycan synthesis, and matrix-degrading activity were analyzed. Incubation of Achilles tendon, Achilles paratenon, and shoulder capsule fibroblasts with ciprofloxacin resulted in a statistically significant 66% to 68% decrease in cell proliferation compared with control cells at day 3 in culture. Ciprofloxacin caused a statistically significant 36% to 48% decrease in collagen synthesis compared with controls in all fibroblast cultures. Ciprofloxacin caused a statistically significant 14% to 60% decrease in proteoglycan synthesis in all fibroblast cell lines. Compared with unstimulated control fibroblasts, culture media from Achilles tendon, paratenon, and shoulder capsule cells that were exposed to ciprofloxacin demonstrated statistically significant increases in matrix-degrading proteolytic activity after 72 hours in culture. This study demonstrates that ciprofloxacin stimulates matrix-degrading protease activity from fibroblasts and that it exerts an inhibitory effect on fibroblast metabolism. The increase in protease activity and the inhibition of both cell proliferation and the synthesis of matrix ground substance may contribute to the clinically described tendinopathies associated with ciprofloxacin therapy.

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