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Relevant bibliographies by topics / Proteolytic enzymes

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Academic literature on the topic 'Proteolytic enzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 August 2024

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Journal articles on the topic "Proteolytic enzymes"

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Chirkin, A. A., O. M. Balaeva-Tikhomirova, V. V. Dolmatova, and I. O. Semenov. "Molecular-structural homology of proteolytic enzymеs in the studying of proteolysis mechanism and its regulation." Proceedings of the National Academy of Sciences of Belarus, Chemical Series 57, no. 2 (June 3, 2021): 206–17. http://dx.doi.org/10.29235/1561-8331-2021-57-2-206-217.

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The actual problem of experimental medicine is the substantiation of new model organisms that meet modern requirements of bioethics, cost and conditions of detention. The aim of this work was a comparative analysis of the homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks. The homology of enzymes in nucleotide sequences in humans and pulmonary freshwater mollusks in the analysis of unregulated proteolysis is 66–68 %; regulated proteolysis – 69–76 %; ubiquitin-like modifiers – 78–83 %; extracellular enzymes – 67–76 %; and intracellular enzymes – 65–72 %. The evolutionary conservatism of proteolytic enzymes and the presence of an open blood circulation, which allows the substances under study to be delivered from the hemolymph directly to target cells, make it possible to use these animals as cheap and convenient test organisms. The practical importance of a sufficiently high homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks justifies the expediency of forming mollusk aquaculture to obtain proteolytic enzyme protein preparations from their tissues within the framework of the tasks of biopharmaceuticals, cosmetics and the food industry.

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de Barros Soares, L. H., D. Ney Marques, P. Melchionna Albuquerque, and M. A. Záchia Ayub. "Influence of some commercial proteases and enzymatic associations on the hydrolytic solubilization of deboned poultry meat proteins Influencia de algunas proteasas comerciales y preparados enzimáticos en la solubilización hidrolitica de las proteínas de la carne de pollo separada mecánicamente." Food Science and Technology International 6, no. 4 (August 2000): 301–6. http://dx.doi.org/10.1177/108201320000600404.

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Mechanically deboned poultry meat (MDPM) was used as a basic source of protein to assess the efficiency of seven proteolytic enzymes and some enzymatic associations over the hydrolysis of that protein. As a main parameter, the evolution of protein solubilization during 4 h of proteolysis was evaluated. The enzymes alcalase, esperase, flavourzyme, fungal protease, HT-proteolytic, papain, proteopex, and combinations of alcalase + flavourzyme, esperase + flavourzyme, HT-proteolytic + flavourzyme, and proteopex + flavourzyme were applied at concentrations of 0.60% and 1.20% of commercial product as a function of total protein. The initial pH was adjusted to 7.0 or 8.0 and the temperature was maintained at 50 °C or 60 °C according to optimal conditions for each enzyme. The proteolytic activities of the enzymes were also compared with azocasein. The hydrolysis index (HI), i.e., the rate between the maximum value and the initial amount of soluble protein was formulated to allow the comparison among treatments. Results showed that the temperature did not influence the proteolysis in the tested model. The association of alcalase + flavourzyme was shown to be more efficient than all other treatments, obtaining more than 70% of soluble protein. Fungal protease pre sented the lowest results.

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Babinets, L. S., K. Y. Kytsai, and V. R. Mykuliak. "The influence of obesity on the parameters of the kallikrein-kinin system and proteolysis in chronic biliary pancreatitis." GASTROENTEROLOGY 58, no. 1 (April 7, 2024): 13–17. http://dx.doi.org/10.22141/2308-2097.58.1.2024.581.

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Background. Clinical practice and science have accumulated data that obese patients suffer from severe forms of acute and chronic pancreatitis, which is explained by the accumulation of fat around the pancreas, a decreased activity of pancreatic enzymes. The purpose of the study is to describe the features of the kallikrein-kinin system and proteolysis in chronic biliary pancreatitis (CBP), depending on the presence of comorbid obesity. Materials and methods. One hundred and thirty-seven patients with chronic biliary pancreatitis were examined and divided into two groups depending on the presence of comorbid obesity: group I consisted of 22 patients with CBP and group II — of 115 patients with CBP and obesity. Results. The obtained results proved that an increase in body weight of patients with CBP lead to a more severe kallikrein-kinin system imbalance, with enhanced activation of inflammation and a decrease in the protective effect of the proteolysis. An increase in the degree of obesity in patients with CBP was accompanied by a more severe kallikrein-kinin system and proteolytic imbalance with an increase in the proteolytic enzymes level that have a damaging effect on the hepatic and pancreatic tissues and have a pro-inflammatory activity, as well as by a decrease in the content of the proteolytic enzyme inhibitors, which reliably weakened the protective effect of kallikrein-kinin system and proteolysis. Conclusions. 1) It was proved that there is a higher activity of the kallikrein-kinin system (according to proteolytic activation and kallikrein levels) and a decrease in the activity of proteolytic enzyme inhibitors (α2-macroglobulin and kininase II) in patients with chronic biliary pancreatitis and comorbid obesity compared to those without obesity (p < 0.05). 2) An increase in the degree of obesity lead to an increase of proteolytic activity and a decrease in the content of the proteolytic enzyme inhibitors in patients with chronic biliary pancreatitis. It was proved the aggravating effect of obesity on the kallikrein-kinin system and proteolytic imbalance, which must be taken into account while forming a comprehensive treatment of such patients.

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Choi, Jin-Ha. "Proteolytic Biosensors with Functional Nanomaterials: Current Approaches and Future Challenges." Biosensors 13, no. 2 (January 21, 2023): 171. http://dx.doi.org/10.3390/bios13020171.

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Proteolytic enzymes are one of the important biomarkers that enable the early diagnosis of several diseases, such as cancers. A specific proteolytic enzyme selectively degrades a certain sequence of a polypeptide. Therefore, a particular proteolytic enzyme can be selectively quantified by changing detectable signals causing degradation of the peptide chain. In addition, by combining polypeptides with various functional nanomaterials, proteolytic enzymes can be measured more sensitively and rapidly. In this paper, proteolytic enzymes that can be measured using a polypeptide degradation method are reviewed and recently studied functional nanomaterials-based proteolytic biosensors are discussed. We anticipate that the proteolytic nanobiosensors addressed in this review will provide valuable information on physiological changes from a cellular level for individual and early diagnosis.

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Salahuddin, Parveen, and Asad U. Khan. "Proteolytic Enzymes Database." Journal of Proteomics & Bioinformatics 01, no. 02 (May 24, 2008): 109–11. http://dx.doi.org/10.4172/jpb.1000017.

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Murphy, G. "PL2.2. Proteolytic enzymes." Cancer Treatment Reviews 34 (2008): 2. http://dx.doi.org/10.1016/j.ctrv.2008.03.016.

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Tikhonov, Sergey L., Natalya V. Tikhonova, Leonid S. Kudryashov, Olga A. Kudryashova, Nadezhda V. Moskovenko, and Irina N. Tretyakova. "Efficiency of Microencapsulation of Proteolytic Enzymes." Catalysts 11, no. 11 (October 21, 2021): 1270. http://dx.doi.org/10.3390/catal11111270.

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Currently, special attention is paid to the study of the effectiveness of the immobilization method—microencapsulation. The aim of the research is to obtain a complex enzyme preparation from pepsin and papain by sequential microencapsulation of enzymes in a pseudo-boiling layer and to evaluate its tenderizing effect on pork. The objects of research were enzymes: pepsin and papain, which were microencapsulated in a protective coating of maltodextrin. It was found that the biocatalytic activity of the complex enzyme preparation is higher than that of pure enzymes. Microencapsulation allows maintaining the high proteolytic activity of enzymes for a long storage period. It has been shown that the thickness of the protective layer during microencapsulation of pepsin and papain in the pseudo-boiling layer of maltodextrin should be in the range of 4–6 microns. During the research, the physicochemical properties of pork were studied depending on the duration of fermentation. It was found that the maximum activity of immobilized enzymes is shifted to the alkaline side. Pork salting with the use of a microencapsulated enzyme preparation in the brine increases the water-binding capacity of proteins to a greater extent in comparison with brine with pure enzymes. The presented data show the high efficiency of sequential microencapsulation of the enzyme pepsin and then papain into a protective layer of maltodextrin in order to preserve their activity during storage.

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Somers, Joanne M., Bernadette O'Brien, William J. Meaney, and Alan L. Kelly. "Heterogeneity of proteolytic enzyme activities in milk samples of different somatic cell count." Journal of Dairy Research 70, no. 1 (February 2003): 45–50. http://dx.doi.org/10.1017/s0022029902005988.

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Milk contains the alkaline proteinase plasmin and lysosomal proteinases; the significance of the latter is ill-defined. The objective of this study was to investigate composition and activities of several different proteolytic enzymes in milk samples of varying somatic cell count (SCC). Increasing milk SCC was correlated with increased plasmin, cathepsin D and cysteine protease activities, with concomitant increases in proteolysis in milk. Addition of plasmin inhibitors confirmed the heterogeneity of proteinase activities in milk, as urea-PAGE analysis of milk samples showed casein hydrolysis in milk after 7 d storage even in samples with inhibitors added; extent and heterogeneity of proteolysis was correlated with milk SCC. Rennet coagulation properties were not significantly correlated with SCC, or activities of measured enzymes. Milk of increasing SCC also exhibited decreased physical stability during incubation of milk at 37 °C. Pasteurized milk was more stable than raw milk, suggesting that the enzyme(s) or mechanisms leading to such instability are impaired by pasteurization. Overall, milk has a very heterogeneous proteolytic enzyme population, with a higher significance of non-plasmin enzymes, such as cathepsin D and cysteine proteinases, than perhaps previously recognised.

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Bergeron, F., R. Leduc, and R. Day. "Subtilase-like pro-protein convertases: from molecular specificity to therapeutic applications." Journal of Molecular Endocrinology 24, no. 1 (February 1, 2000): 1–22. http://dx.doi.org/10.1677/jme.0.0240001.

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Limited proteolysis of most large protein precursors is carried out in vivo by the subtilisin-like pro-protein convertases. Many important biological processes such as peptide hormone synthesis, viral protein processing and receptor maturation involve proteolytic processing by these enzymes, making them potential targets for the development of novel therapeutic agents. However, the efficient development of such molecules requires a better understanding of the molecular mechanisms of proteolytic protein processing. Herein, we review the most recent findings on the molecular aspects of subtilisin-like convertase activity, such as the structural analysis of the proteases, the mechanisms of enzyme/substrate specificity, their interaction with other proteins such as 7B2, and the comparative tissue and cellular distribution of the enzymes and their substrates. These data are then used as a background for the review of the known biological functions of subtilisin-like pro-protein convertases, the reported clinical cases involving proteolytic processing defects and, finally, the ongoing development of new therapeutic inhibitor molecules based on this knowledge.

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ÅGREN, GUNNAR. "Proteins and proteolytic enzymes." Acta Medica Scandinavica 105, no. 1-2 (April 24, 2009): 73–83. http://dx.doi.org/10.1111/j.0954-6820.1940.tb16083.x.

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Dissertations / Theses on the topic "Proteolytic enzymes"

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Ekici, Özlem Doğan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04062004-164633/unrestricted/ekici%5Fozlem%5Fd%5F200312%5Fphd.pdf.

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Ahmed, Naveed. "The synthesis of inhibitors of proteolytic enzymes." Thesis, University of Huddersfield, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.416765.

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Ekici, Ozlem Dogan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Diss., Georgia Institute of Technology, 2003. http://hdl.handle.net/1853/5333.

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Verity, Christiana Kelsick. "Cathepsin D-like aspartic protease from Schistosoma japonicum : developmental, enzymological and immunological studies /." [St. Lucia, Qld.], 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16289.pdf.

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Chaveesuk, Ravipim. "Accleration of fish sauce fermentation using proteolytic enzymes." Thesis, McGill University, 1991. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=60539.

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First grade and second grade Nampla, commercially produced Thai fish sauces, were analyzed for their chemical and microbiological composition. First grade commercially produced Nampla contained higher amounts of total nitrogen, formol nitrogen, free and total amino acids compared to second grade sauce. Most of the essential amino acids were present in both grades of sauces. Low microbial counts of halotolerant microorganisms were observed in both sauces. The use of trypsin and chymotrypsin to accelerate the rate of fish sauce fermentation produced from herring, one of the underutilized fish species in Quebec, was investigated. Results showed that supplementation with trypsin and chymotrypsin increased significantly the rate of proteolysis, the amounts of total nitrogen, formol nitrogen and free amino acids in the final fish sauces (p 0.05). (Abstract shortened by UMI).

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陳臻 and Chun Jade Chan. "Proteolytic enzyme in soy sauce fermentation." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2001. http://hub.hku.hk/bib/B31223977.

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Chan, Chun Jade. "Proteolytic enzyme in soy sauce fermentation." Hong Kong : University of Hong Kong, 2001. http://sunzi.lib.hku.hk:8888/cgi-bin/hkuto%5Ftoc%5Fpdf?B22713384.

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Deane, Shelly May. "Molecular biology studies on the extracellular serine proteases of Vibrio alginolyticus." Doctoral thesis, University of Cape Town, 1989. http://hdl.handle.net/11427/21895.

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Bibliography: pages 161-176.
Vibrio alginolyticus is a gram-negative aerobic bacterium that produces several extracellular serine proteases and a collagenase during the stationary growth phase. The aim of this study was to investigate alkaline serine protease production by this organism, and to attempt the cloning and expression of a V.alginolyticus protease gene in Escherichia coli.

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賴玉耀 and Yuk-yeu William Lai. "Identification and characterization of proteolytic enzymes in Trichinella spp." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1996. http://hub.hku.hk/bib/B31214228.

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Hinchliffe, Paul Stuart. "The synthesis of #beta#-sultam inhibitors of proteolytic enzymes." Thesis, University of Huddersfield, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.368328.

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Books on the topic "Proteolytic enzymes"

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Sterchi, Erwin E., and Walter Stöcker, eds. Proteolytic Enzymes. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6.

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J, Dalling Michael, ed. Plant proteolytic enzymes. Boca Raton, Fla: CRC Press, 1986.

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J, Barrett Alan, Rawlings Neil D, and Woessner J. F, eds. Handbook of proteolytic enzymes. [San Diego, Calif.]: Academic Press, 1998.

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J, Barrett Alan, Rawlings Neil D, and Woessner J. F, eds. Handbook of proteolytic enzymes. 2nd ed. Amsterdam: Elsevier Academic Press, 2004.

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J, Barrett Alan, Rawlings Neil D, and Woessner J. F, eds. Handbook of proteolytic enzymes. San Diego: Academic Press, 1998.

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J, Barrett Alan, Rawlings Neil D, and Woessner J. F, eds. Handbook of proteolytic enzymes. 2nd ed. Amsterdam: Elsevier Academic Press, 2004.

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Westerhof, W., and W. Vanscheidt, eds. Proteolytic Enzymes and Wound Healing. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78891-8.

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J, Beynon R., and Bond Judith S, eds. Proteolytic enzymes: A practical approach. 2nd ed. Oxford: Oxford University Press, 2001.

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J, Beynon R., and Bond Judith S, eds. Proteolytic enzymes: A practical approach. 2nd ed. Oxford: Oxford University Press, 2001.

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J, Beynon R., and Bond Judith S, eds. Proteolytic enzymes: A practical approach. Oxford: IRL Press at Oxford University Press, 1989.

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Book chapters on the topic "Proteolytic enzymes"

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Wong, Dominic W. S. "Proteolytic Enzymes." In Food Enzymes, 124–69. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2349-6_5.

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Garg, S. K., and B. N. Johri. "Proteolytic Enzymes." In Thermophilic Moulds in Biotechnology, 191–218. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-015-9206-2_8.

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Kenny, A. J. "Introduction: Nomenclature and Classes of Peptidases." In Proteolytic Enzymes, 1–8. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_1.

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Polgár, L. "Basic Kinetic Mechanisms of Proteolytic Enzymes." In Proteolytic Enzymes, 148–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_10.

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Knight, C. Graham. "Kinetic Analysis of Protease Inhibition by Synthetic Inhibitors." In Proteolytic Enzymes, 167–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_11.

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Dive, V., J. Jiracek, and A. Yiotakis. "Phosphinic Peptide Libraries for Proteolytic Enzymes." In Proteolytic Enzymes, 188–98. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_12.

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Brömme, Dieter, and Brian F. Schmidt. "Functional Expression of Recombinant Proteases." In Proteolytic Enzymes, 199–229. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_13.

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Kellermann, Josef. "Proteases in Peptide Mapping and Sequencing." In Proteolytic Enzymes, 233–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_14.

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Fontana, Angelo, Patrizia Polverino de Laureto, Vincenzo de Filippis, Elena Scaramella, and Marcello Zambonin. "Limited Proteolysis in the Study of Protein Conformation." In Proteolytic Enzymes, 253–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_15.

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Naim, Hassan Y. "Limited Proteolysis in the Study of Membrane Proteins." In Proteolytic Enzymes, 281–97. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59816-6_16.

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Conference papers on the topic "Proteolytic enzymes"

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Constantinescu, Rodica Roxana, Mariana Ferdes, Madalina Ignat, Ciprian Chelaru, Ana-Maria Ciobanu, and Denis-Andrei Drusan. "Isolation and Characterization of Bacterial Protease Enzyme of Leather Waste." In The 9th International Conference on Advanced Materials and Systems. INCDTP - Leather and Footwear Research Institute (ICPI), Bucharest, Romania, 2022. http://dx.doi.org/10.24264/icams-2022.ii.6.

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The objectives of this study were to isolate and characterize bacteria which produced protease enzyme from tannery solid waste. A solid leather waste sample was used for bacterial isolation, taken from different waste warehouses (solid waste in unhairing phase). Several bacterial strains were isolated from the cultures in Petri dishes, after the growth of the colonies. These strains were characterized in terms of the production of proteolytic enzymes, by a method of screening on the media with casein, which allows the determination of proteolytic indices of microorganisms, the colony diameter, diameter of clear zone, proteolytic index, and enzymatic activities characterization on difference of pH and temperature.

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Menasni, S., W. Hornebeck, L. Robert, and Y. Legrand. "ELASTASE TYPE ACTIVITY OF ENDOTHELIAL CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643360.

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Elastin degrading enzymes have been reported in the vessel wall and both fibroblasts and smooth muscle cells have been shown to produce elastase type enzymes in culture. Data is presented here showing that porcine aortic endothelial cells produce enzyme activities hydrolyzing elastin and synthetic substrates I Sue Ala Ala Ala nitroanilide, SAPNAI considered specific for elastase. Enzyme activity against the SAPNA but not against H-elastin was found to be associated with the cells after triton lysis .This activity was not secreted into the culture medium . The elastolytic activity has been partially characterized in relation to the kinetic of hydrolysis, pH optimum and susceptibility to different inhibitors. These studies revealed the presence of at least two enzymes: a metalo-protease with a pH optimum of 7.5 which accounts for approx. 80% of the total activity, and a serine protease with pH optimum of 8.0 which accounts for the remaining 20% . When the conditioned culture medium was studied, virtually no proteolytic activity could be detected even after activation with an organomercurial agent. However fractionation of the culture medium by gel filtration on HPLC resulted in elastolytic activity both against H-elastin and SAPNA. Proteolytic activity against casein could also be revealed after separation on SDS-PAGE. It is likely that these separation techniques remove an inhibitor also produced by the endothelial cells and allow the expression of proteolytic activity. That the elastolytic activity and the caseinolytic activity revealed by HPLC and PAGE respectively represent the activity of the same enzyme hase not yet been determined, and its relationship to the Stromelysin described by Herron et al(J. Biol. Chem. , 1986, 261. 2810-2813) in rabbit brain capillary endothelial cells is being investigated.

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Tokuyama, Paula Y., Edgar J. Paredes-Gamero, and Antonio Miranda. "Active Leptin Fragments Resistant to Proteolytic Enzymes Present in Human Plasma." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.084.

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Dykes, Samantha S., Henrietta O. Fasanya, and Dietmar W. Siemann. "Abstract 3759: Host and neoplastic cell secretions of proteolytic enzymes potentiate metastasis." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3759.

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Dykes, Samantha S., Henrietta O. Fasanya, and Dietmar W. Siemann. "Abstract 3759: Host and neoplastic cell secretions of proteolytic enzymes potentiate metastasis." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3759.

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Wallace, Robert W., E. Ann Tallant, and Lynn M. Brumley. "POSSIBLE ROLE FOR THE CA2+-DEPENDENT PROTEASE (CALPAIN I) AS AN IRREVERSIBLE ACTIVATOR OF CA2+/CALMODULIN-MEDIATED REACTIONS IN THE HUMAN PLATELET." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644528.

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Calmodulin (CaM)-binding proteins have been identified in human platelets using Western blotting techniques and 125I-CaM. Ten proteins of 245, 225. 175, 150, 90. 82(2), 60 and 41(2) kilodaltons (kDa) bind 125I-CaM in a Ca2+-dependent manner; the binding is blocked by both trifluoperazine and nonradiolabeled CaM. The 225 and 90 kDa proteins are labeled by antisera against myosin light chain kinase (MLCK); the 60 kDa and one of the 82 kDa proteins have been identified as the CaM-dependent phosphatase (calcineurin) and caldesmon. The other proteins are presumed to be other Ca2+/CaM regulated enzymes and proteins which may be important in platelet function. Most of the CaM-binding proteins are degraded upon addition of Ca2+ to a platelet homogenate; the degradation may be blocked by either EGTA, leupeptin or N-ethylmaleimide which suggests that the degradation is due to a Ca2+-dependent protease. Activation of intact platelets under conditions which promote platelet aggregation (i.e. stirring with extracellular Ca2+) also results in limited proteolysis of CaM-binding proteins including those labeled with anti sera against MLCK and the phosphatase. In vitro studies utilizing purified phosphatase and calpain I indicate that the phosphatase is irreversibly activated upon Ca2+-dependent proteolysis. The proteolytically-activated enzyme is insensitive to either Ca2+ or Ca2+/CaM; in addition, its activity in the absence of Ca2+ is even greater than the activity of the unproteolyzed enzyme in the presence of Ca2+ and CaM. Proteolytic stimulation of the phosphatase is accompanied by degradation of the 60 kDa subunit of the enzyme (subunit A) to 56, 52 and 45 kDa fragments, sequentially; proteolysis results in the loss of CaM binding to the enzyme. These results suggest that the Ca2+-dependent protease may have a physiological role in platelet activation as an irreversible activator of Ca2+/ CaM-dependent reactions. Supported by NIH grant HL29766.

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Chepikova, O. E., A. I. Petushkova, I. V. Rodionov, N. V. Gorokhovets, A. A. Zamyatnin Jr, and L. V. Savvateeva. "KINETIC PARAMETERS DETERMINATION OF THE INTERACTIONS BETWEEN CYSTEINE CATHEPSINS AND PEPTIDE INHIBITORS." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-391.

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Excess of cysteine cathepsins activity in tumor microenvironment is caused by violation of their regulation mechanisms. Proteolytic enzymes can hydrolyze endogenous cathepsin inhibitors cystatins. In this study, the interactions between exogenous covalent or non-covalent peptide inhibitors with antitumor activity and recombinant human cysteine cathepsins S and L were studied.

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Varvaresou, A., A. Liatsopoulou, and E. Protopapa. "Proteolytic Enzymes Papain and Chymotrypsin Combined with Laser Techniques for the Management of Facial Hirsutism." In GA – 70th Annual Meeting 2022. Georg Thieme Verlag KG, 2022. http://dx.doi.org/10.1055/s-0042-1759312.

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Blahovec, Ján, Zuzana Kostecká, and Alica Kočišová. "Proteolytic enzymes with endo- and exo-peptidolytic activity in different larval stages of housefly Musca domestica." In Xth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2007. http://dx.doi.org/10.1135/css200709011.

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Ferdes, Mariana, and Rodica Roxana Constantinescu. "Isolation and characterization of fungal and bacterial proteolytic strains from chrome shavings." In The 8th International Conference on Advanced Materials and Systems. INCDTP - Leather and Footwear Research Institute (ICPI), Bucharest, Romania, 2020. http://dx.doi.org/10.24264/icams-2020.ii.9.

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The chrome shavings waste obtained as a result of the leather finishing process accumulates in a large volume in tanneries and represent a major problem for the environment. This waste are particularly resistant to attack of microorganisms, due to the significant concentration of chromium and are thus difficult to degrade. In this study, chrome shavings were analyzed microbiologically by determining the total number of germs and the number of yeasts and molds on specific culture media. Several bacterial and fungal strains were isolated from the cultures in Petri dishes, after the growth of the colonies. These strains were characterized in terms of the production of proteolytic enzymes, by a method of screening on the media with casein, which allows the determination of proteolytic indices of microorganisms. As a result of the tests performed, five bacterial strains probably belonging to the genus Bacillus and two fungal strains from the genera Penicillium and Cladosporium were selected.

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Reports on the topic "Proteolytic enzymes"

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Lewosz, J., A. Kelman, and L. Sequeira. Role of proteolytic enzymes in degradation of plant tissues. Office of Scientific and Technical Information (OSTI), January 1991. http://dx.doi.org/10.2172/6445200.

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Harpaz, Sheenan, Steven G. Hughes, and Pinhas Lindner. Optimization of Diet for Post Larvel/Juvenile Sea Bass and Hybrid Stripped Bass Based on Enzymatic Profiles of their Digestive Tracts. United States Department of Agriculture, December 1995. http://dx.doi.org/10.32747/1995.7604924.bard.

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The overall goal of this research work was to identify the main proteolytic activities which take place in the digestive tracts of young bass fish, and use the knowledge acquired in order to improve feed protein utilization in juvenile fish based on their digestive capacity. The results of the work clearly showed that the young fish possess the entire profile of proteolytic enzymes which is found in adult fish. Yet, in the young fish the level of activity is substantially lower per gram tissue (or gram protein) as compared with the activity found in the digestive tracts of the same fish at an older (larger) age. In addition it was found that the main proteolytic enzyme in these fish is chymotrypsin which accounts for almost 80% of the proteolytic activity. An effort aimed at enhancing this activity has lead to the interesting finding that alcohol substantially enhances the proteolytic activity of fish intestines. Fish intestinal homogenates were used in order to evaluate the suitability of various feeds for the fish. Potential feed proteins were subjected to the proteolytic activity of the fish enzymes in vitro, in a manner simulating the natural process. The proteolytic activity was monitored by the valuation of the products, i.e. amino acid released. This method has proven to be a powerful tool which enables us to predict with a very high degree of accuracy the potential of a feed to promote growth. Selection of feed based on the proteolytic capacity of the fish degestive tracts can now be implemented in feed formulation, as anticipated in the original research proposal.

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Lewosz, J., A. Kelman, and L. Sequeira. The role of proteolytic enzymes in degradation of plant tissues: Summary report. Office of Scientific and Technical Information (OSTI), January 1989. http://dx.doi.org/10.2172/6206504.

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Lewosz, J., A. Kelman, and L. Sequeira. Role of proteolytic enzymes in degradation of plant tissues. Summary of results of studies completed on the prior. Office of Scientific and Technical Information (OSTI), December 1991. http://dx.doi.org/10.2172/10158249.

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Sionov, Edward, Nancy Keller, and Shiri Barad-Kotler. Mechanisms governing the global regulation of mycotoxin production and pathogenicity by Penicillium expansum in postharvest fruits. United States Department of Agriculture, January 2017. http://dx.doi.org/10.32747/2017.7604292.bard.

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The original objectives of the study, as defined in the approved proposal, are: To characterize the relationship of CreA and LaeA in regulation of P T production To understand how PacC modulates P. expansumpathogenicity on apples To examine if other secondary metabolites are involved in virulence or P. expansumfitness To identify the signaling pathways leading to PAT synthesis Penicilliumexpansum, the causal agent of blue mould rot, is a critical health concern because of the production of the mycotoxinpatulin (PAT) in colonized apple fruit tissue. Although PAT is produced by many Penicilliumspecies, the factors activating its biosynthesis were not clear. This research focused on host and fungal mechanisms of activation of LaeA (the global regulator of secondary metabolism), PacC (the global pH modulator) and CreA (the global carbon catabolite regulator) on PAT synthesis with intention to establish P. expansumas the model system for understanding mycotoxin synthesis in fruits. The overall goal of this proposal is to identify critical host and pathogen factors that mechanistically modulate P. expansumgenes and pathways to control activation of PAT production and virulence in host. Several fungal factors have been correlated with disease development in apples, including the production of PAT, acidification of apple tissue by the fungus, sugar content and the global regulator of secondary metabolism and development, LaeA. An increase in sucrose molarity in the culture medium from 15 to 175 mM negatively regulated laeAexpression and PAT accumulation, but, conversely, increased creAexpression, leading to the hypothesis that CreA could be involved in P. expansumPAT biosynthesis and virulence, possibly through the negative regulation of LaeA. We found evidence for CreAtranscriptional regulation of laeA, but this was not correlated with PAT production either in vitro or in vivo, thus suggesting that CreA regulation of PAT is independent of LaeA. Our finding that sucrose, a key ingredient of apple fruit, regulates PAT synthesis, probably through suppression of laeAexpression, suggests a potential interaction between CreA and LaeA, which may offer control therapies for future study. We have also identified that in addition to PAT gene cluster, CreA regulates other secondary metabolite clusters, including citrinin, andrastin, roquefortine and communesins, during pathogenesis or during normal fungal growth. Following creation of P. expansumpacCknockout strain, we investigated the involvement of the global pH regulator PacC in fungal pathogenicity. We demonstrated that disruption of the pH signaling transcription factor PacC significantly decreased the virulence of P. expansumon deciduous fruits. This phenotype is associated with an impairment in fungal growth, decreased accumulation of gluconic acid and reduced synthesis of pectolytic enzymes. We showed that glucose oxidase- encoding gene, which is essential for gluconic acid production and acidification during fruit colonization, was significantly down regulated in the ΔPepacCmutant, suggesting that gox is PacC- responsive gene. We have provided evidence that deletion of goxgene in P. expansumled to a reduction in virulence toward apple fruits, further indicating that GOX is a virulence factor of P. expansum, and its expression is regulated by PacC. It is also clear from the present data that PacC in P. expansumis a key factor for the biosynthesis of secondary metabolites, such as PAT. On the basis of RNA-sequencing (RNA-seq) analysis and physiological experimentation, the P. expansumΔlaeA, ΔcreAand ΔpacCmutants were unable to successfully colonize apples for a multitude of potential mechanisms including, on the pathogen side, a decreased ability to produce proteolytic enzymes and to acidify the environment and impaired carbon/nitrogen metabolism and, on the host side, an increase in the oxidative defence pathways. Our study defines these global regulatory factors and their downstream signalling pathways as promising targets for the development of strategies to fight against this post-harvest pathogen.

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