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)

The human alpha 2-macroglobulin gene was isolated in five overlapping clones. The gene spans approx. 48 kb and consists of 36 exons, from 21 to 229 bp in size and with consensus splice sites. Intron sizes range from 145 bp to 7.5 kb. The alpha 2M gene is a single copy gene in the human genome. A sequence polymorphism within the bait domain, coding for an Arg to His substitution within the primary cleavage site for trypsin, was identified in 1 of 132 individuals tested so far. Three transcription initiation sites have been identified in liver by primer extension and RNase protection assays. The most proximal, major site (+1) is preceded by a TATA-like structure (ATAAA) at -26 bp. Only 2 mRNA species were found in uterus and in cultured lung fibroblasts, while alpha 2M is not expressed to a detectable level in skin fibroblasts. The far distal transcription initiation site which is preceded by an intact TATA box and a potential HP-1 binding site is thus specific for liver.
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PMID:Structure of the human alpha-2 macroglobulin gene and its promotor. 137 37

Twenty Leuconostoc strains isolated from vacuum packaged Vienna-type sausages were screened for antagonistic activity against various Gram-positive organisms (including Listeria spp.). One of the three strains exhibiting inhibitory activity was chosen for further investigation. This strain was identified as Leuc. carnosum and the inhibitory substance produced was named carnosin. Carnosin was inactivated by trypsin but not by catalase or other non-proteolytic enzymes tested. Carnosin retained activity after heating at 100 degrees C for 20 min, whereas heating at 121 degrees C for 15 min resulted in complete loss of activity. Carnosin was active at pH values ranging from 2 to 9. Carnosin activity was not detectable until cells were in the late log-phase of growth. At low temperatures (4 degrees C), higher cell densities were required before carnosin activity could be detected. Carnosin was active against various lactic acid bacteria, Enterococcus faecalis and Enterococcus faecium and against Listeria spp. Difficulties in purification were reduced by growing Leuc. carnosum in a modified MRS medium, having 50% of the normal peptone concentration and no Tween or meat extract. Sodium dodecyl sulphate polyacrylamide gel electrophoresis of partially purified carnosin indicated that it has a molecular mass between 2510 and 6000 Da. Yet, retention of activity after exhaustive dialysis suggested a molecular mass > 14kDa. It is hypothesized that carnosin forms large active complexes which can be dissociated to small (active) components.
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PMID:Characterization and partial purification of a bacteriocin produced by Leuconostoc carnosum LA44A. 144 65

Bacteria isolated from radish were identified as Lactococcus lactis subsp. cremoris R and their bacteriocin was designated lactococcin R. Lactococcin R was sensitive to some proteolytic enzymes (proteinase-K, pronase-E, proteases, pepsin, alpha-chymotrypsin) but was resistant to trypsin, papain, catalase, lysozyme and lipase, organic solvents, or heating at 90 degrees C for 15, 30 and 60 min, or 121 degrees C for 15 min. Lactococcin R remained active after storage at -20 and -70 degrees C for 3 months and after exposure to a pH of 2-9. The molecular weight of lactococcin R was about 2.5 kDa. Lactococcin R was active against many food-borne pathogenic and food spoilage bacteria such as Clostridium, Staphylococcus, Listeria, Bacillus, Micrococcus, Enterococcus, Lactobacillus, Leuconostoc, Streptococcus and Pediococcus spp., but was not active against any Gram-negative bacteria. Lactococcin R was produced during log phase and reached a maximum activity (1600 AU ml-1) at early stationary phase. The highest lactococcin R production was obtained in MRS broth with 0.5% glucose, at 6.5-7.0 initial pH values, 30 degrees C temperature and 18-24-h incubation times. Lactococcin R adsorbed maximally to its heat-killed producing cells at pH 6-7 (95%). Crude lactococcin R at 1280 AU ml-1 was bactericidal, reducing colony counts of Listeria monocytogenes by 99.98% in 3 h. Lactococcin R should be useful as a biopreservative to prevent growth of food-borne pathogenic and food spoilage bacteria in ready-to-eat, dairy, meat, poultry and other food products. Lactococcin R differs from nisin in having a lower molecular weight, 2.5 kDa vs 3.4 kDa, and in being sensitive to pepsin and alpha-chymotrypsin to which nisin is resistant.
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PMID:Detection and characterization of a bacteriocin produced by Lactococcus lactis subsp. cremoris R isolated from radish. 1020 54

Five stains of Bifidobacterium bifidum (ATCC 11863 and 29591, and NCFB 1453, 1454, 1455) were examined for production of bacteriocins in MRS broth with 0.05% cysteine. Only strain NCFB 1454 excreted a bacteriocin into the broth: it was designated bifidocin B. Bifidocin B was sensitive to several proteolytic enzymes (protease IV, pronase E, protease XVII, proteinase K, trypsin, alpha-chymotrypsin, papain, and pepsin), but was resistant to catalase, peroxidase, lipase, lysozyme, cellulase, ribonuclease A, and amylases. It was also resistant to organic solvents such as ethyl alcohol, acetone, hexane, chloroform, methanol, and ether, and to heating at 90 degrees C for 15, 30, and 60 min or at 121 degrees C for 15 min. Bifidocin B remained active after storage at -20 or -7 degrees C for 3 months and retained biological activity after exposure to pH values of 2 to 10. Bifidocin B was active against some food-borne pathogens and food spoilage bacteria such as Listeria, Enterococcus, Bacillus, Lactobacillus, Leuconostoc, and Pediococcus species but was not active against the other gram-positive and gram-negative bacteria tested. Bifidocin B was produced during exponential phase, reaching a maximum activity of 3,200 AU/ml at early stationary phase. Bifidocin B had a molecular mass of about 3.3 kDa as analyzed by Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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PMID:Characterization and antimicrobial spectrum of bifidocin B, a bacteriocin produced by Bifidobacterium bifidum NCFB 1454. 970 52

The ability of Lactococcus lactis subsp. lactis CECT 539 and Pediococcus acidilactici NRRL B-5627 to produce bacteriocins on both diluted and concentrated whey was investigated in batch fermentations. Both strains produced the higher amounts of biomass and bacteriocin titres on diluted whey. Luedeking and Piret expression was able to model the production of nisin, which was produced as a primary metabolite on both culture media. However, the pediocin production could not be typified in any case due to the negligible growth of P. acidilactici. Although the whey supported the growth and bacteriocin production by the two strains, both biomass and bacteriocin productions were lower than those obtained on MRS broth. The effect of total sugar, nitrogen, phosphorous and buffer concentrations on the production of nisin and pediocin was studied in diluted whey using factorial experiments and empirical modelling. The production of nisin was greatly inhibited by the increase in nitrogen, buffer, and to a lesser extent, sugar concentration in the medium, nevertheless, the used phosphorous source produced a light stimulatory effect on bacteriocin synthesis. In addition, the growth of Lc 1.04 was mainly affected by the nitrogen source used. On the other hand, pediocin was inhibited by the increase in buffer, phosphorous, and to a lesser degree, by the sugar and nitrogen concentration. The inhibitory activity of pediocin disappeared almost totally after 15 min of treatment with trypsin, papain, subtilisin and pepsin. The activity of nisin was drastically reduced by treatment with trypsin, subtilisin and pepsin. Nevertheless, 50% of the initial activity was retained when nisin was treated with papain. Both bacteriocins showed the highest heat stability at acidic pH and short incubation times.
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PMID:Nutritional factors affecting the production of two bacteriocins from lactic acid bacteria on whey. 1176 92

Human tear protein profiles were monitored by surface enhanced laser desorption/ionization-time-of-flight mass spectrometry ProteinChip technology (SELDI-TOF ProteinChip) and liquid chromatography-mass spectrometry (LC-MS). Tears were collected from 21 patients scheduled for surgery to remove an ocular surface neoplasm prior to surgery (day 0) and on days 1, 3, and 30 postoperatively. Using this proteomic approach, we verified that three human alpha-defensins (HNP-1, HNP-2, and HNP-3) were significantly up-regulated in their expression after surgery and that their levels decreased to approximately normal by day 30 by which time healing was complete. Further confirmation of the identity of the alpha-defensins in human tears was made by LC purification, trypsin digestion, and ESI-MS/MS analysis of their tryptic digests. The concentrations of HNP-1 and HNP-2 were determined and shown to be markedly increased after ocular surface surgery. The results of the study suggest that human alpha-defensins HNP-1, HNP-2, and HNP-3 are up-regulated after surgery, and may in addition to their antimicrobial properties have an important role in wound healing.
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PMID:Proteomic analysis of human tears: defensin expression after ocular surface surgery. 1525 21

The cell-free supernatant containing bacteriocin ST13BR, produced by Lactobacillus plantarum ST13BR, inhibits the growth of L. casei, Pseudomonas aeruginosa, Enterococcus faecalis, Klebsiella pneumoniae and Escherichia coli. Based on tricine-SDS-PAGE, bacteriocin ST13BR is 10 kDa in size. Complete inactivation or significant reduction in bacteriocin activity was observed after treatment with Proteinase K, trypsin and pronase, but not with catalase or alpha-amylase. Low bacteriocin activity (200 AU/ml) was recorded in BHI medium, M17 broth, 10% (w/v) soy milk, and 2% and 10% (w/v) molasses, despite good growth. Maximal bacteriocin activity (6,400 AU/ml) was recorded after 23 h in MRS broth, but only at 30 degrees C. Tween 80 in MRS broth increased bacteriocin production by more than 50%. Meat extract or yeast extract as sole nitrogen source, or a combination of the two (1 : 1) in MRS broth, stimulated bacteriocin production (6,400 AU/ml). Only 50% activity (3,200 AU/ml) was recorded with tryptone as sole nitrogen source, whereas a combination of tryptone, meat extract and yeast extract yielded 6,400 AU/ml. Bacteriocin production was not stimulated by the addition of glucose at 2.0% w/v (3,200 AU/ml), nor 2% (w/v) fructose, sucrose, lactose or mannose, respectively (800 AU/ml). Activity levels less than 200 AU/ml were recorded in the presence of 0.05% to 0.5% (w/v) maltose. Maximal bacteriocin production (6,400 AU/ml) was recorded in the presence of 2% (w/v) maltose. Maltose at 4.0% (w/v) led to a 50% reduction of bacteriocin activity. The presence of 1.0% (w/v) and higher KH(2)PO(4), or glycerol at 0.2% (w/v) suppressed bacteriocin production.
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PMID:Optimization of bacteriocin production by Lactobacillus plantarum ST13BR, a strain isolated from barley beer. 1548 24

Bacteriocins are natural antimicrobial agents produced by food fermentative bacteria. Lactobacillus acidophilus DSM 20079 produces a small bacteriocin, with a molecular mass of 6.6 kDa, designated acidocin D20079. This antimicrobial peptide was extremely heat-stable (30 min at 121 degrees C) and was active over a wide pH range. It was found to be sensitive to proteolytic enzymes (trypsin, ficin, pepsin, papain, and proteinase K). Acidocin D20079 has a narrow inhibitory spectrum restricted to the genus Lactobacillus which includes L. sakei NCDO 2714, an organism known to cause anaerobic spoilage of vacuum-packaged meat. Maximum production of acidocin D20079 in MRS broth was detected at pH 6.0, and the peptide was purified by ammonium sulphate precipitation followed by sequential cation exchange and hydrophobic interaction chromatography. Purified acidocin D20079 spontaneously formed spherulite crystals during dialysis. As the N-terminus was found to be blocked for sequencing, matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry was used to determine a partial sequence, and the molecular mass of the bacteriocin in the formed crystals (6.6 kDa). Estimates of the molecular weight of the partially purified peptide, using tricine-SDS-PAGE, in which bacteriocin activity was confirmed by overlayer techniques were in accordance with this value.
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PMID:Purification and characterisation of acidocin D20079, a bacteriocin produced by Lactobacillus acidophilus DSM 20079. 1592 17

Lactobacillus acidophilus 88 produced a bacteriocin, designated lactacin F, that demonstrated inhibitory activity toward L. acidophilus 6032, L. lactis 970, L. helveticus 87, L. bulgaricus 1489, L. leichmanii 4797, L. fermentum 1750, and Streptococcus faecalis 19433. Production of lactacin F was pH dependent and could be maximized in MRS broth cultures maintained at pH 7.0. Lactacin F was heat stable and sensitive to ficin, proteinase K, trypsin, and Bacillus subtilis protease. L. acidophilus 88 harbored plasmids of 4 and 27 megadaltons. Variants of L. acidophilus 88 which were deficient in lactacin F production (Laf) and lactacin F immunity (Laf) retained the two resident plasmids. A Laf Laf derivative, L. acidophilus 89, was used as a recipient in agar surface mating experiments with L. acidophilus 88 (Laf Laf). Two types of Laf Laf transconjugants were recovered. One type (T-E) had acquired two plasmids of 68 (pPM68) and 52 (pPM52) megadaltons that were not detected in either the conjugal donor or the other type of Laf Laf transconjugants (T-89). Laf and Laf were unstable in the plasmid-bearing transconjugant. Plasmid analysis of Laf Laf variants revealed that pPM52 and pPM68 were cured with loss of Laf and Laf. Bacteriocin production and immunity phenotypes were genetically stable in Laf Laf transconjugants not harboring pPM52 and pPM68, suggesting chromosomal integration of the transferred determinants. The data demonstrated intragenic conjugation in L. acidophilus and provided direct evidence for involvement of transient plasmid determinants in Laf and Laf.
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PMID:Conjugal Transfer of Plasmid-Encoded Determinants for Bacteriocin Production and Immunity in Lactobacillus acidophilus 88. 1634 4

Lactic acid bacteria were isolated from "Alheira" sausages that have been sampled from different regions in Portugal. The sausages were produced according to different recipes and with traditional starter cultures. Two isolates (HA-6111-2 and HA-5692-3) from different sausages were identified as strains of Pediococcus acidilactici. Each strain produces a bacteriocin, designated as bacHA-6111-2 and bacHA-5692-3. Both bacteriocins are produced at low levels after 18 h of growth in MRS broth (3200 AU/ml against Enterococcus faecium HKLHS and 1600 AU/ml against Listeria innocua N27). BacHA-6111-2 and bacHA-5692-3 are between 3.5 kDa and 6.5 kDa in size, as determined by tricine-SDS-PAGE. Complete inactivation or significant reduction in antimicrobial activity was observed after treatment of cell-free supernatants with proteinase K, pronase and trypsin. No change in activity was recorded when treated with catalase. Both bacteriocins are sensitive to treatment with Triton X-114 and Triton X-100, but resistant to Tween 20, Tween 80, SDS, Oxbile, NaCl, urea and EDTA. The bacteriocins remained stable after 2 h at pH 6.0. A decrease in antibacterial activity was recorded after 60 min at 100 degrees C. After 60 min at 80 degrees C, 60 degrees C and 25 degrees C the antibacterial activity against L. innocua N27 decreased by 25%. Addition of bacHA-6111-2 and bacHA-5692-3 (1600 AU/ml) to a mid-log (5-h-old) culture of L. innocua N27 inhibited growth for 7 h. Addition of the bacteriocins (3200 AU/ml) to a mid-log (5-h-old) culture of E. faecium HKLHS repressed cell growth. The bacteriocins did not adhere to the surface of the producer cells. Both strains contain a 1044 bp DNA fragment corresponding in size to that recorded for pediocin PA-1. Sequencing of the fragments from both bacteriocins revealed homology to large sections of pedA (188 bp), pedB (338 bp) and pedC (524 bp) of pediocin PA-1 and the bacteriocins are considered similar to pediocin PA-1.
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PMID:Characterization of two bacteriocins produced by Pediococcus acidilactici isolated from "Alheira", a fermented sausage traditionally produced in Portugal. 1736 95


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