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Artículos de revistas sobre el tema "Protease"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 25 de julio de 2025

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1

Watanabe, Katsuji, and Koichi Hayano. "Source of soil protease in paddy fields." Canadian Journal of Microbiology 39, no. 11 (1993): 1035–40. http://dx.doi.org/10.1139/m93-157.

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Properties of soil proteases and proteases from Bacillus spp. obtained from water-logged paddy fields treated with organic manure or chemical fertilizer or not treated with fertilizer were compared to elucidate the sources of soil proteases. The major extractable soil proteases were metal chelator sensitive neutral proteases that were active in hydrolyzing benzyloxycarbonyl-L-phenylalanyl-L-leucine and benzyloxycarbonyl-L-phenylalanyl-L-tyrosyl-L-leucine. In this respect they resembled extracellular proteases from Bacillus subtilis (six isolates), Bacillus cereus (four isolates), and Bacillus

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2

Mallia-Milanes, Brendan, Antoine Dufour, Christopher Philp, et al. "TAILS proteomics reveals dynamic changes in airway proteolysis controlling protease activity and innate immunity during COPD exacerbations." American Journal of Physiology-Lung Cellular and Molecular Physiology 315, no. 6 (2018): L1003—L1014. http://dx.doi.org/10.1152/ajplung.00175.2018.

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Dysregulated protease activity is thought to cause parenchymal and airway damage in chronic obstructive pulmonary disease (COPD). Multiple proteases have been implicated in COPD, and identifying their substrates may reveal new disease mechanisms and treatments. However, as proteases interact with many substrates that may be protease inhibitors or proteases themselves, these webs of protease interactions make the wider consequences of therapeutically targeting proteases difficult to predict. We therefore used a systems approach to determine protease substrates and protease activity in COPD airw

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3

Paulin, John P., and Francisco C. Franco. "Modified bis‐tetrahydrofuran inhibitors toward improved binding to HIV‐1 proteases." Vietnam Journal of Chemistry 59, no. 5 (2021): 563–79. http://dx.doi.org/10.1002/vjch.202000179.

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AbstractHIV treatment includes inhibiting HIV‐1 protease which is responsible for viral maturation. However, HIV‐1 protease responds to drug treatment by mutation making the protease‐resistant to inhibitors. In this study, binding interactions between bis‐tetrahydrofuran‐derived (bis‐THF) inhibitors and HIV‐1 protease were described by molecular docking. We characterized the binding energies and all the amino acids present during the binding of the bis‐THF derivatives to the wild type HIV‐1 protease and several mutant HIV‐1 proteases. We found that the modifications to the structure of darunav

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4

Kostallas, George, and Patrik Samuelson. "Novel Fluorescence-Assisted Whole-Cell Assay for Engineering and Characterization of Proteases and Their Substrates." Applied and Environmental Microbiology 76, no. 22 (2010): 7500–7508. http://dx.doi.org/10.1128/aem.01558-10.

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ABSTRACT We have developed a sensitive and highly efficient whole-cell methodology for quantitative analysis and screening of protease activity in vivo. The method is based on the ability of a genetically encoded protease to rescue a coexpressed short-lived fluorescent substrate reporter from cytoplasmic degradation and thereby confer increased whole-cell fluorescence in proportion to the protease's apparent activity in the Escherichia coli cytoplasm. We demonstrated that this system can reveal differences in the efficiency with which tobacco etch virus (TEV) protease processes different subst

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5

Hudig, D., N. J. Allison, T. M. Pickett, U. Winkler, C. M. Kam, and J. C. Powers. "The function of lymphocyte proteases. Inhibition and restoration of granule-mediated lysis with isocoumarin serine protease inhibitors." Journal of Immunology 147, no. 4 (1991): 1360–68. http://dx.doi.org/10.4049/jimmunol.147.4.1360.

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Abstract To kill other cells, lymphocytes can exocytose granules that contain serine proteases and pore-forming proteins (perforins). We report that mechanism-based isocoumarin inhibitors inhibited the proteases and inactivated lysis. When inhibited proteases were restored, lysis was also restored, indicating that the proteases were essential for lysis. We found three new lymphocyte protease activities, "Asp-ase,"Met-ase," and "Ser-ase," which in addition to ly-tryptase and ly-chymase, comprise five different protease activities in rat RNK-16 granules. The general serine protease inhibitor 3,4

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6

Taggart, Clifford, Marcus A. Mall, Gilles Lalmanach, et al. "Protean proteases: at the cutting edge of lung diseases." European Respiratory Journal 49, no. 2 (2017): 1501200. http://dx.doi.org/10.1183/13993003.01200-2015.

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Proteases were traditionally viewed as mere protein-degrading enzymes with a very restricted spectrum of substrates. A major expansion in protease research has uncovered a variety of novel substrates, and it is now evident that proteases are critical pleiotropic actors orchestrating pathophysiological processes. Recent findings evidenced that the net proteolytic activity also relies upon interconnections between different protease and protease inhibitor families in the protease web.In this review, we provide an overview of these novel concepts with a particular focus on pulmonary pathophysiolo

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7

Schuhmann, Holger, Ulrike Mogg, and Iwona Adamska. "A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains." Biochemical Journal 435, no. 1 (2011): 167–74. http://dx.doi.org/10.1042/bj20101613.

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Deg/HtrA proteases are a large group of ATP-independent serine endoproteases found in almost every organism. Their usual domain arrangement comprises a trypsin-type protease domain and one or more PDZ domains. All Deg/HtrA proteases form homo-oligomers with trimers as the basic unit, where the active protease domain mediates the interaction between individual monomers. Among the members of the Deg/HtrA protease family, the plant protease DEG7 is unique since it contains two protease domains (one active and one degenerated) and four PDZ domains. In the present study, we investigated the oligome

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8

Mann, Krin, and Hélène Sanfaçon. "Expanding Repertoire of Plant Positive-Strand RNA Virus Proteases." Viruses 11, no. 1 (2019): 66. http://dx.doi.org/10.3390/v11010066.

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Many plant viruses express their proteins through a polyprotein strategy, requiring the acquisition of protease domains to regulate the release of functional mature proteins and/or intermediate polyproteins. Positive-strand RNA viruses constitute the vast majority of plant viruses and they are diverse in their genomic organization and protein expression strategies. Until recently, proteases encoded by positive-strand RNA viruses were described as belonging to two categories: (1) chymotrypsin-like cysteine and serine proteases and (2) papain-like cysteine protease. However, the functional chara

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9

Karlsson, Anna, Patricia Saravia-Otten, Karin Tegmark, Eva Morfeldt, and Staffan Arvidson. "Decreased Amounts of Cell Wall-Associated Protein A and Fibronectin-Binding Proteins in Staphylococcus aureus sarA Mutants due to Up-Regulation of Extracellular Proteases." Infection and Immunity 69, no. 8 (2001): 4742–48. http://dx.doi.org/10.1128/iai.69.8.4742-4748.2001.

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ABSTRACT Data have been presented indicating that Staphylococcus aureus cell surface protein can be degraded by extracellular proteases produced by the same bacterium. We have found that insarA mutant cells, which produce high amounts of four major extracellular proteases (staphylococcal serine protease [V8 protease] [SspA], cysteine protease [SspB], aureolysin [metalloprotease] [Aur], and staphopain [Scp]), the levels of cell-bound fibronectin-binding proteins (FnBPs) and protein A were very low compared to those of wild-type cells, in spite of unaltered or increased transcription of the corr

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10

Greenfield, Lucy M., Paul W. Hill, Eric Paterson, Elizabeth M. Baggs, and Davey L. Jones. "Do plants use root-derived proteases to promote the uptake of soil organic nitrogen?" Plant and Soil 456, no. 1-2 (2020): 355–67. http://dx.doi.org/10.1007/s11104-020-04719-6.

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Abstract Aims The capacity of plant roots to directly acquire organic nitrogen (N) in the form of oligopeptides and amino acids from soil is well established. However, plants have poor access to protein, the central reservoir of soil organic N. Our question is: do plants actively secrete proteases to enhance the breakdown of soil protein or are they functionally reliant on soil microorganisms to undertake this role? Methods Growing maize and wheat under sterile hydroponic conditions with and without inorganic N, we measured protease activity on the root surface (root-bound proteases) or exogen

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11

Ferrall-Fairbanks, Meghan C., Chris A. Kieslich, and Manu O. Platt. "Reassessing enzyme kinetics: Considering protease-as-substrate interactions in proteolytic networks." Proceedings of the National Academy of Sciences 117, no. 6 (2020): 3307–18. http://dx.doi.org/10.1073/pnas.1912207117.

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Enzymes are catalysts in biochemical reactions that, by definition, increase rates of reactions without being altered or destroyed. However, when that enzyme is a protease, a subclass of enzymes that hydrolyze other proteins, and that protease is in a multiprotease system, protease-as-substrate dynamics must be included, challenging assumptions of enzyme inertness, shifting kinetic predictions of that system. Protease-on-protease inactivating hydrolysis can alter predicted protease concentrations used to determine pharmaceutical dosing strategies. Cysteine cathepsins are proteases capable of c

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12

Hooper, Nigel M. "Proteases: a primer." Essays in Biochemistry 38 (October 1, 2002): 1–8. http://dx.doi.org/10.1042/bse0380001.

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A protease can be defined as an enzyme that hydrolyses peptide bonds. Proteases can be divided into endopeptidases, which cleave internal peptide bonds in substrates, and exopeptidases, which cleave the terminal peptide bonds. Exopeptidases can be further subdivided into aminopeptidases and carboxypeptidases. The Schechter and Berger nomenclature provides a model for describing the interactions between the peptide substrate and the active site of a protease. Proteases can also be classified as aspartic proteases, cysteine proteases, metalloproteases, serine proteases and threonine proteases, d

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13

Alias, Maslinda, Hakim Che Harun Mohammad, Ashraf Razali Nurul, et al. "Production and characterisation of thermostable alkaline protease from Bacillus subtilis isolated from LA hot spring, Terengganu." Research Journal of Biotechnology 16, no. 7 (2021): 84–91. http://dx.doi.org/10.25303/167rjbt8421.

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This research aims to produce thermostable alkaline protease from Bacillus subtilis isolated from La Hot Spring, Terengganu, Malaysia. The study was also conducted to determine the optimum conditions for protease production and stability by considering several parameters including pH, temperature and salt concentration. All seven bacteria were screened on skim milk agar overnight at 37 °C. Three strains with the highest proteolytic activity were identified in protease specific medium. The thermostable alkaline protease had an optimum temperature of 60 °C which achieved 85.73, 82.90 and 83.05 U

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14

Avidano, Michael A., Cheryl S. Cotter, Scott P. Stringer, and Gregory S. Schultz. "Analysis of protease activity in human otitis media." Otolaryngology–Head and Neck Surgery 119, no. 4 (1998): 346–51. http://dx.doi.org/10.1016/s0194-5998(98)70076-2.

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Cronic otitis media is a common problem associated with a nonintact tympanic membrane frequently involving Staphylococcus aureus and Pseudomonas aeruginosa. The virulence of Pseudomonas bacteria is related to the production of two matrix metalloproteinases, elastase and alkaline protease. Serine proteases, such as neutrophil elastase, are produced by the host inflammatory response. These proteases are thought to contribute to tissue destruction and assist bacterial invasion during infection. This preliminary study was done to identify protease activity in otorrhea samples from patients with ot

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15

Su, Hongfei, Zhenlun Xiao, Kefu Yu, et al. "Diversity of cultivable protease-producing bacteria and their extracellular proteases associated to scleractinian corals." PeerJ 8 (May 6, 2020): e9055. http://dx.doi.org/10.7717/peerj.9055.

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Protease-producing bacteria play a vital role in degrading organic nitrogen in marine environments. However, the diversity of the bacteria and extracellular proteases has seldom been addressed, especially in communities of coral reefs. In this study, 136 extracellular protease-producing bacterial strains were isolated from seven genera of scleractinian corals from Luhuitou fringing reef, and their protease types were characterized. The massive coral had more cultivable protease-producing bacteria than branching or foliose corals. The abundance of cultivable protease-producing bacteria reached

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16

Zheng, Xiang, Fangtong Wu, Lu Zhao, et al. "Exploration of Protease Resources in the Gut of Omnivorous Gryllotalpa orientalis (Orthoptera: Gryllotalpidae)." Biology 13, no. 9 (2024): 650. http://dx.doi.org/10.3390/biology13090650.

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An insect’s gut microbiome is an essential “organ” in their life cycle, playing a crucial role by aiding food digestion and nutrient absorption. This study employed both culture-independent and culture-dependent methods to explore the protease resources present in the gut of the omnivorous insect Gryllotalpa orientalis. The findings revealed that the gut extract of G. orientalis contained a diverse array of proteases, including cysteine proteases, pepsin, serine proteases, and trypsin, as well as some unidentified proteases. Furthermore, the protease gene htpX, derived from gut bacterium Pries

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17

Shoari, Alireza. "From Bench to Bedside: Transforming Cancer Therapy with Protease Inhibitors." Targets 3, no. 1 (2025): 8. https://doi.org/10.3390/targets3010008.

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Proteases play a pivotal role in cancer progression, facilitating processes such as extracellular matrix degradation, angiogenesis, and metastasis. Consequently, protease inhibitors have emerged as promising therapeutic agents in oncology. This review provides a comprehensive overview of the mechanisms by which protease inhibitors modulate cancer biology, categorizing inhibitors by their target protease classes, including matrix metalloproteinases, cysteine proteases, and serine proteases. We discuss the therapeutic potential of both synthetic and natural protease inhibitors, highlighting thei

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18

Jairajpuri, Mohamad Aman, and Shoyab Ansari. "Using serpins cysteine protease cross-specificity to possibly trap SARS-CoV-2 Mpro with reactive center loop chimera." Clinical Science 134, no. 17 (2020): 2235–41. http://dx.doi.org/10.1042/cs20200767.

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Abstract Human serine protease inhibitors (serpins) are the main inhibitors of serine proteases, but some of them also have the capability to effectively inhibit cysteine proteases. Severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) main protease (Mpro) is a chymotrypsin-type cysteine protease that is needed to produce functional proteins essential for virus replication and transcription. Serpin traps its target proteases by presenting a reactive center loop (RCL) as protease-specific cleavage site, resulting in protease inactivation. Mpro target sites with its active site serine and

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19

FAMPA, P., C. V. LISBOA, A. M. JANSEN, A. L. S. SANTOS, and M. I. RAMIREZ. "Protease expression analysis in recently field-isolated strains of Trypanosoma cruzi: a heterogeneous profile of cysteine protease activities between TC I and TC II major phylogenetic groups." Parasitology 135, no. 9 (2008): 1093–100. http://dx.doi.org/10.1017/s0031182008004587.

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SUMMARYProtease expression among TCI and TCII field isolates was analysed. Gelatin-containing gels revealed hydrolysis bands with molecular masses ranging from 45 to 66 kDa. The general protease expression profile showed that TCII isolates presented higher heterogeneity compared to TCI. By utilizing protease inhibitors, we showed that all active proteases at acid pH are cysteine-proteases and all proteases active at alkaline pH are metalloproteases. However, the expression of cruzipain, the T. cruzi major cysteine-protease, did not reproduce a heterogeneous TCII cysteine zymogram profile. Dend

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20

Uba, Garba, Muntari Bala, Muhammad Mushidi Abdullah, Muhammad Nor Farhan Saat, Baskaran Gunasekaran, and Mohd Yunus Shukor. "The Application of Crude Ginger Protease as an Inhibitive Assay for Heavy Metals." Journal of Environmental Microbiology and Toxicology 7, no. 1 (2019): 48–53. http://dx.doi.org/10.54987/jemat.v7i1.472.

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In this work, a novel source of protease for the bioassay of heavy metals has been developed using proteases extracted from ginger. The result shows that the optimum protease activity was reached at 1 mg/mL protein concentration of the ginger protease. The optimum casein concentration toward crude ginger protease activity was 1.75 mg/mL. The most suitable pH for protease from crude ginger protease was within the range from pH 5.0 to 7.0. The proteases exhibited high protease activity in a broad range of temperature from 20 to 60 oC. The optimum incubation time for the enzyme occurred at minute

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21

Vuorinen, Emmiliisa, Salla Valtonen, Nazia Hassan, et al. "Protease Substrate-Independent Universal Assay for Monitoring Digestion of Native Unmodified Proteins." International Journal of Molecular Sciences 22, no. 12 (2021): 6362. http://dx.doi.org/10.3390/ijms22126362.

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Proteases are a group of enzymes with a catalytic function to hydrolyze peptide bonds of proteins. Proteases regulate the activity, signaling mechanism, fate, and localization of many proteins, and their dysregulation is associated with various pathological conditions. Proteases have been identified as biomarkers and potential therapeutic targets for multiple diseases, such as acquired immunodeficiency syndrome, cardiovascular diseases, osteoporosis, type 2 diabetes, and cancer, where they are essential to disease progression. Thus, protease inhibitors and inhibitor-like molecules are interest

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22

Das, Kamonashis, Sourav Chakraborty, Mahmudul Hasan, and Abdullah Maruf Rahman Shovo. "In silico analysis to elect superior bacterial alkaline protease for detergent and leather industries." JOURNAL OF ADVANCES IN BIOTECHNOLOGY 5, no. 3 (2015): 685–98. http://dx.doi.org/10.24297/jbt.v5i3.1482.

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Alkaline protease contributes 40% of the total worldwide enzyme sales. Alkaline protease that is stable at very high temperature and pH is massively desirable for detergent industry and leather industry specially in tanning process. So the present study aims to elect superior bacterial alkaline protease (high temperature and pH stable) as compared to the alkaline proteases of currently industrially used bacteria (Bacillus subtilis and Bacillus cereus). A total of 50 protein sequences of alkaline proteases of different bacteria were analyzed through in silico characterization. ProtParam result

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23

El-Shanshoury, Abd El-Raheem R., Mostafa A. El-Sayed, Reda H. Sammour, and Wageeh A. El-Shouny. "Purification and partial characterization of two extracellular alkaline proteases from Streptomyces corchorusii ST36." Canadian Journal of Microbiology 41, no. 1 (1995): 99–104. http://dx.doi.org/10.1139/m95-013.

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Two distinct alkaline proteases were detected in the culture medium of Streptomyces corchorusii ST36 isolated from an Egyptian soil sample. These enzymes were purified by precipitation with chilled ethanol and gel filtration on carboxymethyl Sepharose and on Sephadex G-120. The enzymes were purified 6 and 6.5 fold to homogeneity. The purified enzymes had final specific activities on substrate of 3.6 and 3.9 U/mg. Protease 1 had a molecular mass of 31 kDa and protease 2 was composed of two subunits, of molecular masses 18.6 and 17.4 kDa. The optimal pH and temperature for catalytic activity of

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24

Kuklina, M. M., and V. V. Kuklin. "PROTEASE ACTIVITY IN THE SMALL INTESTINE OF THE NORTHERN FULMAR <i>FULMARUS GLACIALIS</i> BY INFECTION OF <i>TETRABOTHRIUS MINOR</i> (CESTODA: TETRABOTHRIIDAE)." Журнал эволюционной биохимии и физиологии 59, no. 5 (2023): 361–69. http://dx.doi.org/10.31857/s0044452923050054.

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The effect of infection of Tetrabothrius minor (Cestoda: Tetrabothriidae) on the protease activity of the mucous membrane of the small intestine of the Northern Fulmar Fulmarus glacialis was studied. Aspects of changes in the activity of proteases and protease subclasses (metalloproteases, serine proteases and cysteine proteases) by infection of T. minor, and the ability of T. minor to inactivate proteases from the intestinal mucosa and commercial trypsin were evaluated. It has been established that in the localization of T. minor (proximal and medial sections of the small intestine) decreased

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Kim, Chang-Won, Hyun-Seok Kim, Byung-Yong Kim, and Moo-Yeol Baik. "Proteolysis of Defatted Rice Bran Using Commercial Proteases and Characterization of Its Hydrolysates." Food Engineering Progress 15, no. 1 (2011): 41–47. http://dx.doi.org/10.13050/foodengprog.2011.15.1.41.

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The defatted rice bran (DRB) was enzymatically hydrolyzed using eight commercial proteases for 4hr at optimum pH and temperature. Proteolytic hydrolysates were examined in supernatant and precipitate using lowry, semimicro kjeldahl and gravimetric method using weight difference before and after enzymatic hydrolysis. In lowry and kjeldahl protein assay method, two proteases (Alcalase and Protease N) were found to be the most effective enzymes. In gravimetric method, 60.6~118.3 mg protein/g DRB was hydrolyzed after eight commercial proteases treatments. Similar to lowry and kjeldahl method, 118.

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Blusch, Jürgen H., Sigrid Seelmeir, and Klaus von der Helm. "Molecular and Enzymatic Characterization of the Porcine Endogenous Retrovirus Protease." Journal of Virology 76, no. 15 (2002): 7913–17. http://dx.doi.org/10.1128/jvi.76.15.7913-7917.2002.

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ABSTRACT The protease of the porcine endogenous retrovirus (PERV) subtypes A/B and C was recombinantly expressed in Escherichia coli as proteolytically active enzyme and characterized. The PERV Gag precursor was also recombinantly produced and used as the substrate in an in vitro enzyme assay in parallel with synthetic nonapeptide substrates designed according to cleavage site sequences identified in the PERV Gag precursor. The proteases of all PERV subtypes consist of 127 amino acid residues with an M r of 14,000 as revealed by determining the protease N and C termini. The PERV proteases have

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27

Ehrhardt, Katrin, Natalie Steck, Reinhild Kappelhoff, et al. "Persistent Salmonella enterica Serovar Typhimurium Infection Induces Protease Expression During Intestinal Fibrosis." Inflammatory Bowel Diseases 25, no. 10 (2019): 1629–43. http://dx.doi.org/10.1093/ibd/izz070.

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AbstractBackgroundIntestinal fibrosis is a common and serious complication of Crohn’s disease characterized by the accumulation of fibroblasts, deposition of extracellular matrix, and formation of scar tissue. Although many factors including cytokines and proteases contribute to the development of intestinal fibrosis, the initiating mechanisms and the complex interplay between these factors remain unclear.MethodsChronic infection of mice with Salmonella enterica serovar Typhimurium was used to induce intestinal fibrosis. A murine protease-specific CLIP-CHIP microarray analysis was employed to

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Achmad, Ayu Ashari, M. Saifur Rohman, and Irfan D. Prijambada. "Biochemical Properties of Crude Extracellular Proteases from Chromohalobacter salexigens BKL5 and Micrococcus luteus 11A." Indonesian Journal of Biotechnology 21, no. 1 (2017): 56. http://dx.doi.org/10.22146/ijbiotech.26705.

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In this work, we have reported an enzymatic activity and biochemical properties of extracellular proteases from Chromohalobacter salexigens BKL5 and Micrococcus luteus 11A. C. salexigens BKL5 and M. luteus 11A were previously isolated from Bledug Kuwu mud volcano and dietary industry wastewater treatment, respectively. Both bacterial strains were able to produce extracellular proteases, when grown on minimal agar medium supplemented with 1% of skim milk. Proteolytic indexes of C. salexigens BKL5 and M. luteus 11A were 2.5±0.14 and 2.9±0.42, respectively. Both extracellular proteases exhibited

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Tsumura, Kazunobu, and Norihiro Yamada. "Changes in Protease Activity of Ginger Rhizome during Postharvest Storage." Journal of Food Research 14, no. 1 (2024): 42. http://dx.doi.org/10.5539/jfr.v14n1p42.

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It has been reported that ripe ginger rhizomes contain proteolytic enzymes. In this study, we investigated the fluctuations in protease activity from ginger rhizomes stored after harvest for the utilization of proteases. The juice from ginger rhizomes that had been stored for 4 months after harvest exhibited the highest specific protease activity. Additionally, juices with high specific protease activity could form soymilk and cow milk gels. Electrophoresis experiments revealed that the protein bands in ginger rhizome juice were degraded by the proteases contained in the juice. This degradatio

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Gondzik, Veronika, Wolf Michael Weber, and Mouhamed S. Awayda. "Coupling of epithelial Na+ and Cl− channels by direct and indirect activation by serine proteases." American Journal of Physiology-Cell Physiology 303, no. 9 (2012): C936—C946. http://dx.doi.org/10.1152/ajpcell.00395.2011.

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The mammalian collecting duct (CD) is continuously exposed to urinary proteases. The CD expresses an epithelial Na+ channel (ENaC) that is activated after cleavage by serine proteases. ENaC also exists at the plasma membrane in the uncleaved form, rendering activation by extracellular proteases an important mechanism for regulating Na+ transport. Many exogenous and a small number of endogenous extracellular serine proteases have been shown to activate the channel. Recently, kallikrein 1 (KLK1) was shown to increase γENaC cleavage in the native CD indicating a possible direct role of this endog

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Zhu, Yiwen, Jinzhi Song, Xu Zhang, Mengchu Gao, Biyu Peng, and Chunxiao Zhang. "Effect of Electrostatic Interaction between Collagen and Enzymes on Permeation of Protease into the Pelt during Leather Bating Process." Journal of the American Leather Chemists Association 118, no. 10 (2023): 428–38. http://dx.doi.org/10.34314/jalca.v118i10.8231.

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The enzymatic delimed pelts bating process using proteases is critical to improving the overall performance of the leather. Bating effectiveness is determined not only by the properties but also by the permeation behavior of the proteases. Imperfect methods to control protease permeation often results in uneven distribution of enzyme proteins in the pelts, leading to excessive enzymolysis of the surface layer and inadequate opening-up of the inner layer. In this study, the relative size of proteases and delimed pelts were analyzed, the permeation behavior of fluorescein-labeled proteases in th

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Safitri, A., SN Ethica, S. Tanoeyadi, et al. "Potential of Protease of Marine Bacterium Bacillus sp. HSFI-9 as Lysis Reagent in DNA Extraction of Blood and Buccal Cells." IOP Conference Series: Earth and Environmental Science 1478, no. 1 (2025): 012013. https://doi.org/10.1088/1755-1315/1478/1/012013.

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Abstract Proteases produced by microorganisms, including Bacillus sp., have been widely reported to have economic and environmental advantages. The utilization of proteases from bacteria in varied environments has grown rapidly and has played an important role as a lysis reagent in various molecular tests and diagnostics. The potential of local bacterial proteases is promising as a biocatalyst in protein breakdown reactions, which is also vital in DNA extraction. It can be an alternative lower-cost reagent of commercial Proteinase-K. Dependence on imports of protease reagents poses significant

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Li, Qingxin, and Congbao Kang. "Structure and Dynamics of Zika Virus Protease and Its Insights into Inhibitor Design." Biomedicines 9, no. 8 (2021): 1044. http://dx.doi.org/10.3390/biomedicines9081044.

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Zika virus (ZIKV)—a member of the Flaviviridae family—is an important human pathogen. Its genome encodes a polyprotein that can be further processed into structural and non-structural proteins. ZIKV protease is an important target for antiviral development due to its role in cleaving the polyprotein to release functional viral proteins. The viral protease is a two-component protein complex formed by NS2B and NS3. Structural studies using different approaches demonstrate that conformational changes exist in the protease. The structures and dynamics of this protease in the absence and presence o

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Fu, Runzhong, Wannita Klinngam, Martin Heur, Maria C. Edman, and Sarah F. Hamm-Alvarez. "Tear Proteases and Protease Inhibitors." Eye & Contact Lens: Science & Clinical Practice 46 (March 2020): S70—S83. http://dx.doi.org/10.1097/icl.0000000000000641.

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Liu, Ying, Jun Ying An, Xu Qiong Hu, and Chun Hou Xu. "Isolation and Identification of Thermophilic Protease Bacterium 0701 and its Protease Characterization." Advanced Materials Research 781-784 (September 2013): 1032–36. http://dx.doi.org/10.4028/www.scientific.net/amr.781-784.1032.

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Soil was collected from Huguangyan of Zhanjiang city and regarded as separate material, It was screened thermophilic protease-producing bacteria though dilution flat, transparent circle and Folin method. Strain 0701 isolated was identificated by its morphological features, physiological and biochemical characteristics and 16s rRNA. This experiment also researched on the genetic stability of enzyme producing, and different temperature, pH influence on proteases activity. 25 high temperature-tolerance protease producing strains were isolated, which accounted for 28.1 % of all the isolated strain

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Hook, V. Y. H., and S. R. Hwang. "Novel Secretory Vesicle Serpins, Endopin 1 and Endopin 2: Endogenous Protease Inhibitors with Distinct Target Protease Specificities." Biological Chemistry 383, no. 7-8 (2002): 1067–74. http://dx.doi.org/10.1515/bc.2002.115.

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Abstract Secretory vesicles of neuroendocrine cells possess multiple proteases for proteolytic processing of proteins into biologically active peptide components, such as peptide hormones and neurotransmitters. The importance of proteases within secretory vesicles predicts the presence of endogenous protease inhibitors in this subcellular compartment. Notably, serpins represent a diverse class of endogenous protease inhibitors that possess selective target protease specificities, defined by the reactive site loop domains (RSL). In the search for endogenous serpins in model secretory vesicles o

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Lebuan, Urbanus Yustus, Roga Florida Kembaren, Merry Meryam Martgrita, and Cut Rizlani Kholibrina. "Thrombolytic protease characterization from leaves and fruit flesh of the jernang rattan plant (Daemonorops draco)." Indonesian Journal of Biotechnology 28, no. 4 (2023): 248. http://dx.doi.org/10.22146/ijbiotech.82390.

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Thrombolytic agents are used for thrombolytic therapy to dissolve blood clots that form in a blood vessel. All currently used thrombolytic agents have unfavorable shortcomings, such as gastrointestinal bleeding, allergic reactions, and thrombolytic agent resistance, treatment for some of which can be quite expensive. As a result, the search for thrombolytic agents derived from plants is currently taking place. Some plants have been discovered to contain protease enzymes with thrombolytic activity; pharmaceuticals derived from plants are believed to be safer. Jernang rattan (Daemonorops draco)

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Saipriya, S. *1, and Kumar Chava 2. Vijay. "HOST PROTEASE INHIBITION BY SPECIFIC PATHOGENS IN PERIODONTAL DISEASE." International Journal of Research - Granthaalayah 6, no. 4 (2018): 131–37. https://doi.org/10.5281/zenodo.1242613.

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Proteolytic tissue degradation is a typical phenomenon in chronic inflammatory periodontal disease with the uncontrolled release of host and bacterial derived proteases causing self-digestion and tissue destruction. Antimicrobial proteins and peptides constitute a diverse class of host defense molecules that act early to combat invasion and infection with bacteria and other microorganisms and protease inhibitors forms one of the functional classes of antimicrobial peptides. Plasma protease inhibitors present in gingival crevicular fluid as well as tissues may play a critical role in the protec

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Weeda, Sarah M., G. N. Mohan Kumar, and N. Richard Knowles. "Correlative changes in proteases and protease inhibitors during mobilisation of protein from potato (Solanum tuberosum) seed tubers." Functional Plant Biology 37, no. 1 (2010): 32. http://dx.doi.org/10.1071/fp09188.

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Potato tubers (Solanum tuberosum L.) contain protease inhibitors that function in plant defence and as storage proteins. A multi-domain cysteine protease inhibitor, potato multicystatin (PMC), has also been implicated in regulating protein accumulation in developing tubers by inhibiting proteases. Unlike developing tubers, sprouting tubers mobilise protein reserves to support growth of developing plants and, therefore, show an increase in protease activity. Using single-eye containing cores (seedcores) from seed tubers, we characterised the relative changes in patatin, PMC, proteases and serin

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Strachecka, A. J., M. M. Gryzińska, M. Krauze, and K. Grzywnowicz. "Profile of the body surface proteolytic systém in Apis mellifera quee." Czech Journal of Animal Science 56, No. 1 (2011): 15–22. http://dx.doi.org/10.17221/150/2009-cjas.

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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

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Chourasia, P., B. Patel, M. M. Prakash, and S. Gaherwal. "Screening and Optimization of Extracellular Alkaline Protease Production from Bacillus Spp." Environment Conservation Journal 13, no. 3 (2012): 49–52. http://dx.doi.org/10.36953/ecj.2012.130309.

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Protease enzyme catalyzes the hydrolysis of protein. Among the various proteases, bacterial proteases are most significant when compared with animal and fungal proteases. In the present study a protease producing bacteria were isolated from soil collected from Govt. Holkar Science College, Indore campus and identified as Bacillus spp. They were grown within a temperature range between 25°C & 45 °C and pH range of 6.0 to 11.0. The optimum condition for protease production obtained was 35 °C at pH 9. The best carbon and organic nitrogen sources for this bacterial strain were fructose and yea

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Serrano-Luna, José de Jesús, Isaac Cervantes-Sandoval, Jesús Calderón, Fernando Navarro-García, Victor Tsutsumi, and Mineko Shibayama. "Protease activities of Acanthamoeba polyphaga and Acanthamoeba castellanii." Canadian Journal of Microbiology 52, no. 1 (2006): 16–23. http://dx.doi.org/10.1139/w05-114.

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Acanthamoeba spp. are free-living amoebae that cause amoebic granulomatous encephalitis, skin lesions, and ocular amoebic keratitis in humans. Several authors have suggested that proteases could play a role in the pathogenesis of these diseases. In the present work, we performed a partial biochemical characterization of proteases in crude extracts of Acanthamoeba spp. and in conditioned medium using 7.5% SDS–PAGE copolymerized with 0.1% m/v gelatin as substrate. We distinguished a total of 17 bands with proteolytic activity distributed in two species of Acanthamoeba. The bands ranged from 30 t

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Park, Jung-Ho, Yoshihiro Yamaguchi, and Masayori Inouye. "Intramolecular Regulation of the Sequence-Specific mRNA Interferase Activity of MazF Fused to a MazE Fragment with a Linker Cleavable by Specific Proteases." Applied and Environmental Microbiology 78, no. 11 (2012): 3794–99. http://dx.doi.org/10.1128/aem.00364-12.

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ABSTRACTThe genomes of human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV) consist of single-stranded RNA encoding polyproteins, which are processed to individual functional proteins by virus-encoded specific proteases. These proteases have been used as targets for drug development. Here, instead of targeting these proteases to inhibit viral infection, we utilized the protease activity to activate a toxic protein to prevent viral infection. We engineered the MazE-MazF antitoxin-toxin system ofEscherichia colito fuse a C-terminal 41-residue fragment of antitoxin MazE to the

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Wei, Yang, Mingdong Huang, and Longguang Jiang. "Advancements in Serine Protease Inhibitors: From Mechanistic Insights to Clinical Applications." Catalysts 14, no. 11 (2024): 787. http://dx.doi.org/10.3390/catal14110787.

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Serine proteases, a significant class of enzymes comprising approximately one-third of known human proteases, are ubiquitously present across various organisms. These enzymes typically exhibit highly conserved catalytic domain structures, and their activity is stringently regulated within the body, playing a pivotal role in numerous physiological processes. Dysregulation of serine protease activity can result in severe consequences, including excessive inflammation, heightened risk of thrombosis and cancer, and even mortality. Serine protease inhibitors have emerged as critical regulators, off

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Tyagi, R. D., V. Sikati Foko, S. Barnabe, A. S. Vidyarthi, J. R. Valéro, and R. Y. Surampalli. "Simultaneous production of biopesticide and alkaline proteases by Bacillus thuringiensis using sewage sludge as a raw material." Water Science and Technology 46, no. 10 (2002): 247–54. http://dx.doi.org/10.2166/wst.2002.0344.

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The simultaneous production of Bacillus thuringiensis (Bt) based biopesticide and proteases was studied using synthetic medium and wastewater sludge as a raw material. The studies were conducted in shake flask and computer controlled 15-L capacity fermentors. Measuring viable cell and spore counts, entomotoxicity and protease activity monitored the progress of the biopesticide production process. A higher viable cell count and spore count was observed in synthetic Soya medium, however, higher entomotoxicity and protease activity were observed in wastewater sludge medium. Thus, the wastewater s

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Sakoda, Yoshihiro, Natalie Ross-Smith, Toru Inoue, and Graham J. Belsham. "An Attenuating Mutation in the 2A Protease of Swine Vesicular Disease Virus, a Picornavirus, Regulates Cap- and Internal Ribosome Entry Site-Dependent Protein Synthesis." Journal of Virology 75, no. 22 (2001): 10643–50. http://dx.doi.org/10.1128/jvi.75.22.10643-10650.2001.

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ABSTRACT Virulent and avirulent strains of swine vesicular disease virus (SVDV), a picornavirus, have been characterized previously. The major determinants for attenuation have been mapped to specific residues in the 1D-2A-coding region. The properties of the 2A proteases from the virulent and avirulent strains of SVDV have now been examined. Both proteases efficiently cleaved the 1D/2A junction in vitro and in vivo. However, the 2A protease of the avirulent strain of SVDV was much less effective than the virulent-virus 2A protease at inducing cleavage of translation initiation factor eIF4GI w

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Menou, Awen, JanWillem Duitman, Pauline Flajolet, Jean-Michel Sallenave, Arnaud André Mailleux, and Bruno Crestani. "Human airway trypsin-like protease, a serine protease involved in respiratory diseases." American Journal of Physiology-Lung Cellular and Molecular Physiology 312, no. 5 (2017): L657—L668. http://dx.doi.org/10.1152/ajplung.00509.2016.

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More than 2% of all human genes are coding for a complex system of more than 700 proteases and protease inhibitors. Among them, serine proteases play extraordinary, diverse functions in different physiological and pathological processes. The human airway trypsin-like protease (HAT), also referred to as TMPRSS11D and serine 11D, belongs to the emerging family of cell surface proteolytic enzymes, the type II transmembrane serine proteases (TTSPs). Through the cleavage of its four major identified substrates, HAT triggers specific responses, notably in epithelial cells, within the pericellular an

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Mintoo, Mubashir, Amritangshu Chakravarty, and Ronak Tilvawala. "N-Terminomics Strategies for Protease Substrates Profiling." Molecules 26, no. 15 (2021): 4699. http://dx.doi.org/10.3390/molecules26154699.

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Proteases play a central role in various biochemical pathways catalyzing and regulating key biological events. Proteases catalyze an irreversible post-translational modification called proteolysis by hydrolyzing peptide bonds in proteins. Given the destructive potential of proteolysis, protease activity is tightly regulated. Dysregulation of protease activity has been reported in numerous disease conditions, including cancers, neurodegenerative diseases, inflammatory conditions, cardiovascular diseases, and viral infections. The proteolytic profile of a cell, tissue, or organ is governed by pr

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Howng, Bruce, Michael B. Winter, Carol LePage, Irina Popova, Michael Krimm, and Olga Vasiljeva. "Novel Ex Vivo Zymography Approach for Assessment of Protease Activity in Tissues with Activatable Antibodies." Pharmaceutics 13, no. 9 (2021): 1390. http://dx.doi.org/10.3390/pharmaceutics13091390.

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Proteases are involved in the control of numerous physiological processes, and their dysregulation has been identified in a wide range of pathologies, including cancer. Protease activity is normally tightly regulated post-translationally and therefore cannot be accurately estimated based on mRNA or protein expression alone. While several types of zymography approaches to estimate protease activity exist, there remains a need for a robust and reliable technique to measure protease activity in biological tissues. We present a novel quantitative ex vivo zymography (QZ) technology based on Probody

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Kryvalap, Yury, та Jan Czyzyk. "The Role of Proteases and Serpin Protease Inhibitors in β-Cell Biology and Diabetes". Biomolecules 12, № 1 (2022): 67. http://dx.doi.org/10.3390/biom12010067.

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Regulation of the equilibrium between proteases and their inhibitors is fundamental to health maintenance. Consequently, developing a means of targeting protease activity to promote tissue regeneration and inhibit inflammation may offer a new strategy in therapy development for diabetes and other diseases. Specifically, recent efforts have focused on serine protease inhibitors, known as serpins, as potential therapeutic targets. The serpin protein family comprises a broad range of protease inhibitors, which are categorized into 16 clades that are all extracellular, with the exception of Clade

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