Relevant bibliographies by topics / Phenylmethylsulfonyl fluoride; Serine protease

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Academic literature on the topic 'Phenylmethylsulfonyl fluoride; Serine protease'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Phenylmethylsulfonyl fluoride; Serine protease"

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Lopez-Llorca, L. V. "Purification and properties of extracellular proteases produced by the nematophagous fungus Verticillium suchlasporium." Canadian Journal of Microbiology 36, no. 8 (1990): 530–37. http://dx.doi.org/10.1139/m90-093.

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The fungal parasite of eggs of cyst nematodes, Verticillium suchlasporium, produced extracellular proteases when grown in semiliquid culture with gelatin as the only source of nitrogen and carbon. The proteolytic activity of culture filtrates was maximum 12–14 days after inoculation. Gel filtration chromatography in Sephadex G-100 resolved two peaks of proteolytic activity. The peak accounting for most of the activity was further purified by ion-exchange chromatography in SP-Sephadex C-25 as a single peak. This protease had a molecular mass of 32 kDa calculated by sodium dodecyl sulfate – poly
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Manavalan, Tamilvendan, Arulmani Manavalan, Shiyamsundar Ramachandran, and Klaus Heese. "Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium-TK1 for the Detergent and Leather Industry." Biology 9, no. 12 (2020): 472. http://dx.doi.org/10.3390/biology9120472.

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An increased need by the green industry for enzymes that can be exploited for eco-friendly industrial applications led us to isolate and identify a unique protease obtained from a proteolytic Bacillus megaterium-TK1 strain from a seawater source. The extracellular thermostable serine protease was processed by multiple chromatography steps. The isolated protease displayed a relative molecular weight (MW) of 33 kDa (confirmed by zymography), optimal enzyme performance at pH 8.0, and maximum enzyme performance at 70 °C with 100% substrate specificity towards casein. The proteolytic action was blo
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Zaqueo, Kayena D., Anderson M. Kayano, Rodrigo Simões-Silva, et al. "Isolation and Biochemical Characterization of a New Thrombin-Like Serine Protease fromBothrops pirajaiSnake Venom." BioMed Research International 2014 (2014): 1–13. http://dx.doi.org/10.1155/2014/595186.

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This paper presents a novel serine protease (SP) isolated fromBothrops pirajai, a venomous snake found solely in Brazil that belongs to the Viperidae family. The identified SP, named BpirSP-39, was isolated by three chromatographic steps (size exclusion, bioaffinity, and reverse phase chromatographies). The molecular mass of BpirSP-39 was estimated by SDS-PAGE and confirmed by mass spectrometry (39,408.32 Da). The protein was able to form fibrin networks, which was not observed in the presence of serine protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF). Furthermore, BpirSP-39 p
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Deane, D., L. Inglis, and D. Haig. "The 175 antigen expressed on myeloid and erythroid cells during differentiation is associated with serine protease activity." Blood 85, no. 5 (1995): 1215–19. http://dx.doi.org/10.1182/blood.v85.5.1215.bloodjournal8551215.

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Monoclonal antibody 175 recognizes a cell-surface antigen on more than 80% of nucleated ovine bone marrow cells (BMC). The distribution is unusual, as the majority of differentiated myeloid and erythroid cells express the antigen (175 antigen), whereas mast cells, basophils, and the majority of lymphocytes do not. The level of 175 antigen expression has been shown to increase as BMC differentiate during hematopoiesis. Previous attempts to identify the 175 antigen have been unsuccessful. In this study, the 175 antigen was affinity-purified and shown to contain serine protease activity. Immunobl
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Wang, Wei, Guoqing Peng, Jingjing Sun, Chengcheng Jiang, Jianhua Hao, and Xiu Zhang. "Screening and Characterization of Marine Bacillus atrophaeus G4 Protease and Its Application in the Enzymatic Hydrolysis of Sheep (Ovis aries) Placenta for the Preparation of Antioxidant Peptides." Molecules 30, no. 10 (2025): 2217. https://doi.org/10.3390/molecules30102217.

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Proteolytic enzymes, which play a crucial role in peptide bond cleavage, are widely applied in various industries. In this study, protease-producing bacteria were isolated and characterized from marine sediments collected from the Yellow Sea, China. Comprehensive screening and 16S rDNA sequencing identified a promising G4 strain as Bacillus atrophaeus. Following meticulous optimization of fermentation conditions and medium composition via response surface methodology, protease production using strain G4 was significantly enhanced by 64%, achieving a yield of 3258 U/mL. The G4 protease exhibite
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Buckmaster, M. J., J. A. Curci, P. R. Murray, et al. "Source of Elastin-Degrading Enzymes in Mycotic Aortic Aneurysms: Bacteria or Host Inflammatory Response?" Cardiovascular Surgery 7, no. 1 (1999): 16–26. http://dx.doi.org/10.1177/096721099900700106.

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Elastolytic matrix metalloproteinases play a central role in the development of chronic atherosclerotic aortic aneurysms, but mycotic aortic aneurysms are a distinct and unusual form of aneurysm disease caused by bacterial infection. Mycotic aortic aneurysms follow a more rapid and unpredictable course than chronic aneurysm disease and they exhibit a predilection for the suprarenal aorta, further implying unique pathophysiologic mechanisms. The purpose of this study was to examine the nature and source of elastin-degrading enzymes in mycotic aortic aneurysm. Bacterial isolates and aortic tissu
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Khan, Hidayatullah, Irshad Ali, Arif-ullah Khan, et al. "Purification and Biochemical Characterization of Alkaline Serine Protease from Caesalpinia bonducella." Natural Product Communications 5, no. 6 (2010): 1934578X1000500. http://dx.doi.org/10.1177/1934578x1000500625.

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A high molecular weight serine protease has been purified to electrophoretic homogeneity from the seeds of Caesalpinia bonducella Flem. (Caesalpiniaceae) by the combination of size exclusion and ion exchange chromatography. About 524 fold purification was achieved with an overall recovery of 6.8%. The specific activity was found to be 86 U/mg/min at pH 8.0. The calculated Km and Vmax were 1.66 mg/mL and 496.68 units/min per mg of protein, respectively. The molecular mass was estimated to be about 63 kDa by sodium dodecyl sulfate PAGE. The enzyme showed optimum activity at pH 8.0 and exhibited
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Khan, Naveed A., Edward L. Jarroll, Noorjahan Panjwani, Zhiyi Cao, and Timothy A. Paget. "Proteases as Markers for Differentiation of Pathogenic and Nonpathogenic Species ofAcanthamoeba." Journal of Clinical Microbiology 38, no. 8 (2000): 2858–61. http://dx.doi.org/10.1128/jcm.38.8.2858-2861.2000.

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Acanthamoeba keratitis is a vision-threatening infection caused by pathogenic species of the genusAcanthamoeba. Although not allAcanthamoeba spp. can cause keratitis, it is important to differentiate pathogenic species and isolates from nonpathogens. Since extracellular proteases may play a role in ocular pathology, we used colorimetric, cytopathic, and zymographic assays to assess extracellular protease activity in pathogenic and nonpathogenicAcanthamoeba. Colorimetric assays, using azo-linked protein as a substrate, showed extracellular protease activity in Acanthamoeba-conditioned medium an
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Ajamhassani, Maryam, Arash Zibaee, Jalal Sendi, Hassan Askary, and Nasser Farrar. "Proteolytic Activity in the Midgut of the Crimson Speckled Moth Utethesia Pulchella L. (Lepidoptera: Arctiidae)." Journal of Plant Protection Research 52, no. 3 (2012): 368–73. http://dx.doi.org/10.2478/v10045-012-0061-0.

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Proteolytic Activity in the Midgut of the Crimson Speckled MothUtethesia PulchellaL. (Lepidoptera: Arctiidae)Samples were prepared from the midgut of 4th instar larvae of the crimson speckled mothUtethesia pulchellaL. to find proteolytic activity and properties. Result revealed the presence of high proteolytic activity in the midgut when taking into account specific proteinases including trypsin-like, chymotrypsin-like, elastase and two exopeptidase (aminopeptidase and carboxipeptidase). The optimal pH of general protease was 8 and 7 when using azocasein and hemoglobin as general substrates, r
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Cui, Hongxia, Liping Wang, and Yang Yu. "Production and Characterization of Alkaline Protease from a High Yielding and Moderately Halophilic Strain of SD11 Marine Bacteria." Journal of Chemistry 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/798304.

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A marine bacterium SD11, which was isolated from sea muds (Geziwo Qinhuangdao Sea area, China), was used to produce thermostable alkaline serine nonmetal protease in the skim milk agar plate medium with 10% NaCl. The optimal temperature about the manufacture of the extracellular protease was ~60°C. The crude enzyme was stable at 20–50°C. The activity was retained to 60% and 45% after heating for 1 h at 60 and 70°C, respectively. The protease was highly active in a wide pH scope (8.0–10.0) and maximum protease activity exhibited at pH 10.0. The activity was restrained by phenylmethylsulfonyl fl
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Dissertations / Theses on the topic "Phenylmethylsulfonyl fluoride; Serine protease"

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Espirito, Santo Alexandre Ribeiro do. "Efeitos de alterações geneticas e ambientais sobre a birrefringencia da matriz organica do esmalte dentario." [s.n.], 2008. http://repositorio.unicamp.br/jspui/handle/REPOSIP/290015.

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Orientador: Sergio Roberto Peres Line<br>Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Odontologia de Piracicaba<br>Made available in DSpace on 2018-08-10T16:39:26Z (GMT). No. of bitstreams: 1 EspiritoSanto_AlexandreRibeirodo_D.pdf: 9422040 bytes, checksum: 9034465ff462c933a4d9d5ab9721b610 (MD5) Previous issue date: 2008<br>Resumo: O esmalte envolve a porção coronária dos dentes e constitui a estrutura mais mineralizada do corpo vertebrado. Seu desenvolvimento tem início com secreção, processamento proteolítico e auto-agregação de uma complexa mistura de proteínas. O est
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VOTTARIELLO, FRANCESCA. "OLIGOMERIZATION OF RNase A:a) A STUDY OF THE INFLUENCE OF SERINE 80 RESIDUE ON THE 3D DOMAIN SWAPPING MECHANISMb) “ZERO-LENGTH” DIMERS OF RNase A AND THEIR CATIONIZATION WITH PEI." Doctoral thesis, 2010. http://hdl.handle.net/11562/344075.

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"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide
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