Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Previous work has demonstrated that Gardnerella vaginalis can utilize catalase as a sole source of iron. In this study, the interaction between G. vaginalis cells and catalase was investigated. G. vaginalis cells were shown to bind digoxigenin (DIG)-labeled catalase using a solid phase dot blot assay. An increase in catalase binding was observed from cells grown under iron-restrictive conditions. Western blot analysis of G. vaginalis proteins resulted in the detection of a putative catalase-binding protein with an estimated molecular mass of 128 kDa. The 128-kDa catalase-binding protein was not detected from intact G. vaginalis cells treated with trypsin prior to Western blot analysis suggesting this protein may be surface-exposed.
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PMID:Binding of catalase by Gardnerella vaginalis. 1103 78

Strains of Lactobacillus isolated from dairy products and genital tract competed with Candida albicans through a membrane of 12000 dalton cut-off. This inhibition was due to hydrogen peroxide and was trypsin-stable, heat-sensitive and antagonized by catalase. Lactobacillus coming from "starters" showed antimicrobial activity against fungus isolated in a yogurt factory. Penicillium, Alternaria, Phialophora, Microsporum and Candida spp. were inhibited when 10(2) spores were inoculated in the assay. No inhibition was observed with 10(5) spores. Besides, one of 21 Lactobacillus strains isolated from the vaginas of healthy women inhibited pathogenic bacteria by means a bacteriocin trypsin-sensitive, heat-stable and retained by dialysis membrane. Tablets for future probiotic use were prepared and the viability of bacteria was assayed using media with different compositions. Pharmaceutical preparations with polyethyleneglycol was the best formulation for the Lactobacillus viability, the counts remained between 10(7) and 10(6) cfu/tablet for up to 1 year.
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PMID:Conservation in probiotic preparations of Lactobacillus with inhibitory capacity on other species. 1106 31

The aims of the present study were to screen and characterize the antimicrobial lactic acid bacteria which were isolated from healthy oral cavities of Thai volunteers, and to characterize their inhibiting substances. Among 3790 isolates (suspected to be lactic acid bacteria) from 130 volunteers, five showed an appreciable effect against Sarcina lutea ATCC 9341, Bacillus cereus ATCC 11778, Escherichia coli ATCC 25922, Staphylococcus aureus ATCC 6538, Streptococcus mutans DTMU 1, Strep. salivarius DTMU 1, Strep. sanguis DTMU 1, Candida albicans ATCC 13803 and C. albicans DTMU 2, as well as the oral pathogens. These antimicrobial isolates included L17 and N14 which showed the antibacterial activity, D14 which showed the anticandidal activity, and D6 and N8 which showed both the antibacterial and anticandidal activities. The isolates were later found to be facultative anaerobic, Gram-positive, non-spore-forming, non-capsule-forming and catalase-negative bacilli. They could utilize casein but could not hydrolyse starch, and they produced hydrogen peroxide and bacteriocins. Their antimicrobial potentials were found to be affected by pH, catalase, proteolytic enzymes and temperature. The activity was partially inactivated after catalase treatment, significantly declined at pH > or =9.0 or after trypsin and pepsin treatments, and also reduced after heating at > or =100 degrees C. However, the antimicrobial activity of these five isolates was somewhat resistant to heat. When the isolates were tested for their antimicrobial sensitivity, they were shown to be sensitive to a number of antimicrobial agents. The final identification revealed that D6, D14 and N14 were Lactobacillus paracasei subsp. paracasei, and L17 and N8 were Lact. rhamnosus.
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PMID:Lactic acid bacteria from healthy oral cavity of Thai volunteers: inhibition of oral pathogens. 1116 19

A new species, Porphyromonas gulae sp. nov., is proposed to include strains isolated from the gingival sulcus of various animal hosts which are distinct from related strains of Porphyromonas gingivalis of human origin. This bacterium exhibits the following characteristics: black-pigmented colonies; asaccharolytic, obligate anaerobic growth; and Gram-negative, non-motile and non-spore-forming, rod-shaped cells. Colonies do not fluoresce under UV light. Vitamin K1 and haemin are required for growth. Cells haemagglutinate sheep erythrocytes. Major fatty acid end products are butyric acid, isovaleric acid, succinic acid and phenylacetic acid. Strains are catalase-positive and indole is produced. Alkaline phosphatase, trypsin-like and N-acetyl-beta-glucosaminidase activities are strong. A beta-galactosidase and a glutamylglutamic acid arylamidase are also present. The G+C content of the chromosomal DNA is 51 mol%. DNA-DNA homology data and 16S rRNA gene sequence analysis provide strong evidence that strains from the animal biotype of P. gingivalis represent a Porphyromonas species that is distinct from P. gingivalis. The type strain of P. gulae is Loup 1T (= ATCC 51700T = NCTC 13180T).
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PMID:Porphyromonas gulae sp. nov., an anaerobic, gram-negative coccobacillus from the gingival sulcus of various animal hosts. 1141 86

During a screening for bacteria producing enzymes with peroxidase activity, a Bacillus sphaericus strain was isolated. This strain was found to contain an intracellular enzyme with peroxidase activity. The native enzyme had a molecular mass of above 300 kDa and precipitated at a salt concentration higher than 0.1 M. Proteolytic digestion with trypsin reduced the molecular mass of the active enzyme to 13 kDa (dimer) or 26 kDa (tetramer) and increased its solubility, allowing purification to homogeneity. Spectroscopic investigations showed the enzyme to be a hemoenzyme containing heme c as the covalently bound prosthetic group. The enzyme was stable up to 90 degrees C and at alkaline conditions up to pH 11, with a pH optimum at pH 8.5. It could be visualized by activity staining after SDS-PAGE and showed activity with a number of typical substrates for peroxidases, e.g., 2,2'-azino-bis(3-ethylbenz-thiazoline-6-sulfonic acid) diammonium salt, guaiacol and 2,4-dichlorophenol; however the enzyme had no catalase and cytochrome c peroxidase activity.
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PMID:Isolation and characterization of a thermostable intracellular enzyme with peroxidase activity from Bacillus sphaericus. 1149 Oct 81

Several serine proteases are directly cytotoxic. We investigated whether the cytotoxic effects of proteases are associated with increased levels of reactive oxygen species (ROS) in cells. We found that treatment of lung fibroblasts or bronchial epithelial cells with relatively high concentrations (0.1--100 U/ml) of neutrophil elastase, trypsin, and Pronase increased ROS levels in the mitochondria and cytoplasm. The protease-induced increase in ROS was associated with oxidative cellular injury as determined by generation of 8-hydroxy-2'-deoxyguanosine and malonaldehyde plus 4-hydroxyalkenal. The protease-induced increase in ROS was not merely due to cell detachment because the proteases also caused an increase in ROS in suspended cells, which precluded attachment to the extracellular matrix. The protease-induced increase in ROS appears to contribute to cytotoxicity because cell death induced by proteases was attenuated by treatment with catalase, a decomposer of H(2)O(2), and accelerated by treatment with aminotriazole, a catalase inhibitor. These results suggest that several proteases increase oxidative stress, indicating a direct interaction between proteases and ROS in mediating cytotoxicity.
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PMID:Serine proteases increase oxidative stress in lung cells. 1150 81

An immunofluorescence staining method for Epon-embedded materials is described. Rat kidney and liver were fixed by perfusion with 1% glutaraldehyde for 10 min. Tissue slices were embedded in Epon. Semithin sections with thicknesses ranging from 1,000 to 100 nm were cut and mounted on clean glass slides. Epoxy resin was removed by treatment with 10% sodium ethoxide. Sections were digested with 0.05% trypsin and then treated with sodium borohydride. Sections were immunostained for leucine aminopeptidase (plasma membrane), catalase (peroxisomes), 3-ketoacyl-CoA thiolase (mitochondria), cathepsin D (lysosomes), and LGP107 (lysosomal membrane) using Cy(2)- or Alexa 546-labeled secondary antibodies. In 1,000-nm-thick sections, non-specific fluorescence remained and such fluorescence decreased as the sections became thinner. Clear specific fluorescence was obtained in the sections with thicknesses ranging from 250 to 100 nm with Alexa 546-labeled antibody (red fluorescence) but was not specific enough with Cy(2)- or Alexa 430-labeled antibody (green fluorescence). Sodium borohydride greatly abolished autofluorescence of glutaraldehyde. The present method made it possible to obtain signals in cross-sections of biological materials with a thickness of 250-100 nm, which are difficult to obtain in optical section using a confocal laser microscope.
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PMID:Immunofluorescence technique for 100-nm-thick semithin sections of Epon-embedded tissues. 1181

Phycomyces blakesleeanus isocitrate lyase (EC 4.1.3.1) is in vivo reversibly inactivated by hydrogen peroxide. The purified enzyme showed reversible inactivation by an ascorbate plus Fe(2+) system under aerobic conditions. Inactivation requires hydrogen peroxide; was prevented by catalase, EDTA, Mg(2+), isocitrate, GSH, DTT, or cysteine; and was reversed by thiols. The ascorbate served as a source of hydrogen peroxide and also reduced the Fe(3+) ions produced in a "site-specific" Fenton reaction. Two redox-active cysteine residues per enzyme subunit are targets of oxidative modification; one of them is located at the catalytic site and the other at the metal regulatory site. The oxidized enzyme showed covalent and conformational changes that led to inactivation, decreased thermal stability, and also increased inactivation by trypsin. These results represent an example of redox regulation of an enzymatic activity, which may play a role as a sensor of redox cellular status.
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PMID:Specific and reversible inactivation of Phycomyces blakesleeanus isocitrate lyase by ascorbate-iron: role of two redox-active cysteines. 1192 12

The ability of Prevotella nigrescens to utilize and bind to hemoglobin was investigated. Growth studies showed that P. nigrescens was able to utilize hemoglobin efficiently as an iron source. Binding of P. nigrescens to hemoglobin was demonstrated by dot blot assay. Heat and trypsin treatments of the bacteria led to a decrease in activity. Globin gave nearly complete inhibition of activity. Additionally, lactoferrin partially inhibited activity. In contrast, transferrin, cytochrome C and catalase exerted little or no inhibitory effect. Although the sugars tested did not affect activity, several of the amino acids tested, including arginine, cysteine, histidine and lysine, inhibited activity. In a solid phase assay, 41-, 56- and 59-kDa proteins of P. nigrescens reacted with hemoglobin. These results suggest that P. nigrescens utilizes hemoglobin for growth and 41-, 56- and 59-kDa proteins may be involved in hemoglobin binding.
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PMID:Characterization of binding and utilization of hemoglobin by Prevotella nigrescens. 1203 Sep 67

An understanding of digestibility in marine fish larvae is required to formulate a diet to replace zooplankton. Using flounder, this study was aimed at determining which digestive enzymes are synthesized in the larval pancreas, and how the proteins are cleaved in the digestive canal. Whole mount in situ hybridization indicated that the mRNA of all digestive enzyme precursors examined, including trypsin, chymotrypsin, elastase, carboxypeptidase A and B, and lipase, was expressed in the pancreas of first feeding larvae at 3 days post-fertilization. In the larvae before differentiation of the stomach, protein digestion in the digestive canal mainly depends on pancreatic proteases. So, to evaluate protein digestibility in the larval digestive canal, the digestion of proteins by pancreatic extract was monitored by gel electrophoresis. It was indicated that thyroglobulin, albumin and lactate dehydrogenase were rapidly cleaved to polypeptide fragments, but ferritin and catalase exerted resistance to proteolysis, suggesting that digestibility in the larval digestive canal differs depending on protein species.
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PMID:mRNA expression of pancreatic enzyme precursors and estimation of protein digestibility in first feeding larvae of the Japanese flounder, Paralichthys olivaceus. 1204 72


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