Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Many properties have been assigned to the procollagen and properdin (Type I) modules of thrombospondin-1 (TSP1) based on activities of large proteolytic fragments of TSP1 or peptides containing TSP1-derived sequences. To examine the activities of the modules more exactly, we expressed the first properdin module (P1); the third properdin module (P3); the first and second properdin modules (P12); the first, second, and third properdin modules (P123); and the procollagen module with the first, second, and third properdin modules (CP123) in the GELEX expression vector (GE1) using the baculovirus system. GE1 encodes the pre-pro sequence, the transglutaminase cross-linking site(s), the protease-sensitive site, and the gelatin binding domain from the amino terminus of rat fibronectin. All five recombinant proteins were expressed by insect cells, secreted into the culture medium, and purified by gelatin-agarose affinity chromatography. P123 shared with TSP1 a resistance to trypsin unless reduced and alkylated. P12/GE1, P123/GE1, and CP123/GE1 bound poorly to heparin-agarose except in the absence of sodium chloride, whereas peptides based on P2 are known to bind to heparin in up to 150 mM sodium chloride. In cross-linking experiments employing activated recombinant factor XIII and the transglutaminase cross-linking site in the fibronectin-derived sequence, P12/GE1, P123/GE1, CP123/GE1, and P3/GE1 but not P1/GE1 became incorporated into a fibrin clot more than GE1 alone. Analysis of the complex indicated that cross-linking was to the portion of the fibrin alpha-chain remaining in the D-dimer of plasmin digests. P123 also cross-linked to the Aalpha-chain of unclotted fibrinogen. P123 competed for 125I-TSP1 incorporation into the fibrin clot. P123 did not cross-link to plasminogen, histidine-rich glycoprotein, fibronectin, or plasma globulins other than fibrinogen/fibrin. These results indicate that the properdin modules of TSP1 specifically interact with fibrinogen/fibrin but not with heparin under physiologic conditions.
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PMID:Interaction of recombinant procollagen and properdin modules of thrombospondin-1 with heparin and fibrinogen/fibrin. 986 61

Formation of the preinitiation complex for adenovirus DNA replication involves the incoming preterminal protein-adenovirus DNA polymerase heterodimer being positioned at the origin of replication by protein-DNA and protein-protein interactions. Preterminal protein directly binds to the cellular transcription factor nuclear factor III (Oct-1), via the POU homeodomain. Co-precipitation of POU with individual domains of preterminal protein expressed by in vitro translation indicated that POU contacts multiple sites on preterminal protein. Partial proteolysis of preterminal protein in the presence or absence of POU homeodomain demonstrated that many sites accessible to proteases in free preterminal protein were resistant to cleavage in the presence of POU homeodomain. The accessibility of sites in free preterminal protein to cleavage by trypsin was strongly dependent on the ionic strength, suggesting that preterminal protein may undergo a sodium chloride-induced conformational change. It is therefore likely that the POU homeodomain contacts a number of sites on preterminal protein to induce a conformational change which may influence the initiation of adenovirus DNA replication.
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PMID:Characterisation of the adenovirus preterminal protein and its interaction with the POU homeodomain of NFIII (Oct-1). 1037 99

Graft copolymer networks of poly(methacrylic acid-g-ethylene glycol) were prepared by free radical solution UV-polymerization of methacrylic acid (MAA) and poly(ethylene glycol) monomethacrylate. Dynamic swelling studies indicated that complexation/decomplexation processes occurred due to hydrogen bonding between the carboxylic groups of the poly(methacrylic acid) (PMAA) and the ether groups of poly(ethylene glycol) (PEG). The effects of copolymer composition, graft chain molecular weight, environmental pH and ion content on network structure and gel behavior were studied. The largest change in swelling ratio and mesh size of the gel structure was observed in gels containing the highest content of PEG and the longest molecular weight PEG grafts. Complexation was greatest in hydrogels containing the longest PEG grafts and equimolar amounts of MAA and PEG. The swelling was much less pronounced in the presence of calcium chloride compared to sodium chloride which could be attributed to the complexation of calcium of the carboxylic groups in the polymer. The copolymers showed significant but less binding of calcium compared to poly(acrylates) like Carbopol 934P and polycarbophil. The P(MAA-g-EG) copolymers inhibited trypsin but to a lesser extent than the known protease inhibitors Carbopol 934P and polycarbophil. Results suggest that P(MAA-g-EG) copolymers are good drug delivery carrier candidates due to their pH-sensitive and controllable swelling behavior. Additionally, they possess some protease inhibition effect along with their bioadhesive properties which make them promising carriers for peptides or proteins.
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PMID:Complexation graft copolymer networks: swelling properties, calcium binding and proteolytic enzyme inhibition. 1050 71

In observations of the movements of the infective third-stage larvae of a rodent parasitic nematode, Strongyloides ratti, on a sodium chloride gradient set up on agarose plates, two types of chemokinetic behavior were seen: a unidirectional avoidance movement on initial placement of the larvae in unfavorable environmental conditions and a random dispersal movement on their placement within an area of favorable conditions. Track patterns were straight in the avoidance movement but included multiple changes of direction and loops in the dispersal movement. In the present study we examined the interventional activity of treatment with various enzymes, lectins, and chemicals by analyzing the unidirectional avoidance movements of the larvae. We observed that beta-glucosidase, hyaluronidase, beta-galactosidase, trypsin, protease, lipase, phospholipase C, soybean agglutinin, wheat germ agglutinin, and spermidine exerted inhibitory actions on those movements, which may be guided by the chemosensory function of this nematode.
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PMID:Effects of various treatments on the chemokinetic behavior of third-stage larvae of Strongyloides ratti on a sodium chloride gradient. 1109 92

An improved size-exclusion chromatography (SEC) was developed to isolate extremely basic (alkaline) proteins, such as trypsin (pI=10.5), lysozyme (pI=11), and histone (pI=10.8). Develosil 300 Diol-5 (300 x 8 mm I.D., 30 nm average pore diameter) column was used with an eluent of 0.1 M sodium phosphate, 1.5 M sodium chloride, glycerol (40%, v/v), 2-propanol (10%, v/v), and Brij-58 (1%, v/v). Under these conditions, the final apparent pH becomes to 4.0, and pH adjustment is not necessary. Column temperature and flow rate were 15 degrees C and 0.2 ml/min, respectively. This elution system is stable and reliable, and applications onto human pancreatic juice, human bile, and tissue homogenates were successfully achieved. Since this system is convenient for protein analysis, it is expected to be generally applicable to clinical and biochemical research for identifying protein components in combination with microsequencing.
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PMID:Size-exclusion chromatography of biological samples which contain extremely alkaline proteins. 1283 74

Ultrasound energy has been applied to speed up enzymatic hydrolysis processes of mussel tissue in order to determine trace and ultratrace elements (As, Al, Cd, Cr, Cu, Fe, Mn, Ni, Pb, Zn). The element releases, by action of three proteases (pepsin, pancreatin, trypsin), lipase, and alpha-amylase, have been evaluated by inductively coupled plasma atomic emission spectrometry. Different variables such as pH, sonication temperature, ionic strength, hydrolysis time, ultrasound frequency, extracting volume, and enzyme mass were simultaneously studied by applying an experimental design approach (Plackett-Burman design and central composite design). Results showed that the hydrolysis time was statistically nonsignificant (confidence interval of 95%) for most of the elements and enzymes, meaning that the hydrolysis procedure can be finished within a 30-60-min range. These hydrolysis times are far shorter than those obtained when using thermostatic cameras, between 12 and 24 h. Statistically significant factors were the ultrasound frequency (the highest metals releasing at high-ultrasound frequency), pH, sonication temperature, and ionic strength. All metals can be extracted using the same operating conditions (pH of 1.0 and sodium chloride at 1.0% for pepsin; pH of 7.5, temperature at 37 degrees C, and 0.4 M potassium dihydrogen phosphate/potassium hydrogen phosphate buffer for amylase; pH of 8.0 and 0.5 M potassium dihydrogen phosphate/potassium hydrogen phosphate buffer for pancreatin; pH of 5.0 and 0.5 M potassium dihydrogen phosphate/potassium hydrogen phosphate buffer for lipase; pH of 8.0 and 0.2 M potassium dihydrogen phosphate/potassium hydrogen phosphate buffer for trypsin). Analytical performances, such as limits of detection and quantification, repeatability of the overall procedure, and accuracy, by analyzing DORM-1, DORM-2, and TORT-1 certified reference materials, were finally assessed for each enzyme.
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PMID:Ultrasound bath-assisted enzymatic hydrolysis procedures as sample pretreatment for the multielement determination in mussels by inductively coupled plasma atomic emission spectrometry. 1522 23

A novel thermophilic, coccoid methanogen isolated from nonthermal freshwater sediments is described. Hydrogen plus carbon dioxide and formate were substrates for methanogenesis, and methane production was stimulated by yeast extract, Casamino Acids, and tryptose. Growth also occurred autotrophically. Elevated levels of sodium chloride were not required for maximum growth and were inhibitory above 2%. The minimum doubling time occurred at 57 degrees C, and the upper and lower limits for methane production were 62 and 26 degrees C, respectively. The optimum pH for growth was between 7.0 and 7.5. Inhibitory antibiotics included metronidazole, anisomycin, chloramphenicol, and lasalocid. Colonies were circular, dark yellow, shiny, and convex with entire edges. Cells were 1 to 2.5 mum in diameter, nonmotile, occurring singly or in pairs, and fimbriated. Cells were lysed by pronase or trypsin digestion, glass-distilled water, and 1% sodium dodecyl sulfate. Electron micrographs of thin sections showed a monolayered cell wall ca. 20 nm thick. The DNA base ratio was 49.2 mol% guanine plus cytosine. The whole cell protein pattern differed from that of other named coccoid methanogens.
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PMID:Isolation and characterization of a novel thermophilic, freshwater methanogen. 1634 76

Soluble proteins from the salt-tolerant Rhizobium etli strain EBRI 26 were separated by two-dimensional (2D) gel electrophoresis and visualised by Commassie staining. Six proteins are highly expressed after induction by 4% NaCl compared to the non-salt-stressed cells. These proteins have pI between 5 and 5.5 and masses of approximately 22, 25, 40, 65, 70, and 95 kDa. These proteins were analysed by Matrix-assisted laser adsorption ionization time of flight (MALDI-TOF) after digestion with trypsin. Despite having very good peptide mass fingerprint data, these proteins could not be identified, because the genome sequence of R. etli is not yet published. In a second approach, soluble proteins from salt-induced or non-salt-induced cultures from R. etli strain EBRI 26 were separately labelled with different fluorescent cyano-dyes prior to 2D difference in gel electrophoresis. Results revealed that 49 proteins are differentially expressed after the addition of sodium chloride. Fourteen proteins are overexpressed and 35 were downregulated. The genome of Sinorhizobium meliloti, a closely related species to R. etli, has been published. Similar experiments using Sinorhizobium meliloti strain 2011 identified four overexpressed and six downregulated proteins. Among the overexpressed protein is a carboxynospermidin decarboxylase, which plays an important role in the biosynthesis of spermidin (polyamine). The enzyme catalase is among the downregulated proteins. These proteins may play a role in salt tolerance.
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PMID:A proteomic approach towards the analysis of salt tolerance in Rhizobium etli and Sinorhizobium meliloti strains. 1660 15

To test the hypothesis (Plant Physiology 59: 155-157) that monocotyledons contain a unique oligomycin-insensitive ATPase, we prepared submitochondrial particles and a soluble fraction from sonicated corn mitochondria (Zea mays L. cv. Earliking). Although the ATPase activity of the whole sonicate was relatively insensitive to oligomycin, the corn submitochondrial particles possessed an ATPase activity that was nearly completely inhibited by oligomycin, and was activated by trypsin. This ATPase is similar to that from other sources (plants, animals, and microorganisms). The soluble fraction also contained an active ATPase, which was inhibited by azide and stimulated by sodium chloride and trypsin. The soluble fraction differed from other F(1)-ATPases in that it was cold-stable.
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PMID:Oligomycin-sensitive ATPase of Submitochondrial Particles from Corn. 1666 Mar 37

Of 131 bacterial isolates from seaweed, a culture of Bacillus licheniformis produced a novel protein with antibacterial activity against methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and Listeria monocytogenes. The antibacterial activity was maximal in cultures prepared in Columbia broth containing pieces of synthetic polyurethane sponge and shaken at 210 to 230 rpm. Antibacterial activity was not found in cultures grown statically or with different speeds of rotary shaking. Reduced activity was apparent in supernatants prepared from marine 2216E broth and tryptone soya broth with or without 1% (wt/vol) sodium chloride. The antibacterial compound was sensitive to proteinase K, pronase, and trypsin, but was not affected by Tween-20, -40, -60, or -80, or alpha- or beta-amylase. Activity was not adversely affected by heating up to 40 degrees C or treatment at pH 5 to 14. The bioactive compound was determined to be associated with a protein of 30.7 kDa, which had homology to the YbdN protein of B. licheniformis ATCC 14580.
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PMID:Recovery and characterization of a 30.7-kDa protein from Bacillus licheniformis associated with inhibitory activity against methicillin-resistant Staphylococcus aureus, vancomycin-resistant enterococci, and Listeria monocytogenes. 1679 53


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