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)

Outer membrane proteins extracted from isolated cell walls of Proteus mirabilis were able to combine the cell wall phospholipids in a model membrane system. The presence of outer membrane proteins in vesicular model membranes mediated the release of previously entrapped [14C]sucrose while [3H]inulin was retained. Incorporation of lipopolysaccharide from the same cell walls was not required for the formation of such selectively permeable membranes. Three major outer membrane proteins of apparent molecular weights 39000, 36000 and 17000 were isolated using acetic acid and sodium deoxycholate solution as solvents and avoiding the strongly denaturing sodium dodecyl sulfate. The isolated proteins were assayed for their ability to form hydrophilic pores in reconstituted membranes. The trypsin-sensitive 39000-Mr protein and the peptidoglycan-associated 36000-Mr protein were equally effective in this function whereas the 17000-Mr protein mediated little penetration of low molecular weight solute. The 39000-Mr and 36000-Mr proteins also protected reconstituted membrane vesicles from disruption by detergent while 17000-Mr protein was ineffective in this regard.
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PMID:Reconstitution of model membranes from phospholipid and outer membrane proteins of Proteus mirabilis. Role of proteins in the formation of hydrophilic pores and protection of membranes against detergents. 33 2

An antibiotic-producing bacterium repeatedly isolated from human feces was characterized by standard bacteriological methods. The bacterium is a gram-positive bacillus possessing morphological and physiological features similar to those of Bacillus subtilis, except that it lacks temperature-resistant spore formation and has peritrichous flagella. The cell-free antibiotic produced by the organism in vitro was effective against some gram-negative and gram-positive bacteria and yeast in minimum inhibitory concentration and antibiotic disk assays. The 1,200-dalton antibiotic had an optimal activity against Proteus vulgaris within the pH range of 5.7 to 6.8. The activity was totally destroyed by digestion with pronase and trypsin but was resistant to pepsin, chymotrypsin, papain, and nuclease digestion. In addition, the antibiotic activity against P. vulgaris was stable between pH 3 to 9 and within the temperature range of 20 to 100 degrees C when tested in the fermentation medium. The activity was only partially retained by membrane filters which normally retain globular proteins of molecular weights between 500 to 10,000. Electrophoresis in phosphate buffer indicated that the activity against P. vulgaris had an isoelectric point of approximately 6.45. These properties are compatible with the antibiotic activity associated with a small peptide.
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PMID:Identification of an antibiotic-producing bacterium from the human intestinal tract and characterization of its antimicrobial product. 62 95

The sharing of one and possibly two or more non-type-specific antigens by most strains of groups A, C, and G streptococci is described. With the exception of a single strain of Proteus mirabilis, this antigen(s) was not found among strains of groups B and D streptococci, coagulase-positive staphylococci, Escherichia coli, Pseudomonas sp., and Salmonella sp. The non-type-specific antigen(s) could not be separated from M protein by fractionation with various saturations of ammonium sulfate or by column chromatography with calcium hydroxylapatite even though the latter method allowed the recovery of a fraction of M protein which was free of the cross-reactive antigen(s). The resistance of this non-type-specific antigen(s) to hot acid extraction and its sensitivity to treatment with trypsin differentiate it from the T and R antigens of group A streptococci, both of which are trypsin resistant. Co-precipitation of both type-and non-type-specific antigens occurred with type-specific antiserum and suggested that the type- and non-type-specific antigens represent either different, covalently bonded antigenic determinants on the same protein or different proteins noncovalently linked together.
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PMID:Characterization of a non-type-specific antigen(s) associated with group A streptococcal type 12 M protein. 80 25

Proteocines derived from twelve previously described bacteriocinogenic strains of Proteus mirabilis and Proteus vulgaris were investigated. All proteocine preparations were particulate, unaffected by trypsin, and destroyed by freezing and thawing or by heating at 60 degrees C for 30 minutes. Proteocine activity was removed by adsorption with the appropriate sensitive organisms. The active principles of all preparations were partially purified by precipitation with 70% (w/v NH4(SO4)2 followed by ultra-centrifugation. Column chromatography showed that proteocine activity was associated with only one of the peaks of material which absorbed strongly at 257 mu. All twelve proteocine preparations were revealed by electron microscopy as a phage-tail-like structure and each particle had a sheath, a core, and a base-plate from which spine-like fibres extend. Adsorption of these particles to the cell wall of sensitive strains did not disrupt the bacterial cell wall, but the cytoplasmic membrane and the cell contents shrank, with consequent death of the "infected" cell.
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PMID:Physical properties and the fine structure of proteocines. 98 32

Cell walls of Proteus mirabilis in the stationary phase of growth contain a lipoprotein in covalent linkage to peptidoglycan and probably also in free form in the outer membrane. The protein moiety of this lipoprotein is composed of about 50 amino acids and has an approximate molecular weight of 5500. The Proteus lipoprotein has glycine and phenylalanine as specific components which are not present in lipoproteins of other enteric bacteria. Treatment of the peptidoglycan-lipoprotein complex of Proteus with trypsin leaves lysine as the only lipoprotein amino acid attached to the peptidoglycan. This suggests that in P. mirabilis, as in Escherichia coli, the lipoprotein is linked to the peptidoglycan by its C-terminal lysine residue.
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PMID:Amino-acid composition of the covalent rigid-layer lipoprotein in cell walls of Proteus mirabilis. 110 Apr 5

An enzyme immunoassay for detection of bacterial antigens in urine specimens from urinary tract infections (UTI) was developed. The antigens detected in infections by Enterobacteriaceae: Escherichia coli, Enterobacter aerogenes, and Proteus sp. were different from the enterobacterial common antigen (ECA). They were digested by trypsin and were characterized by remarkable thermostability; their molecular weights were approximately 34,000 and 31,000. They were detected by means of antisera to ECA or to suspension of E. coli. The frequency of positive results with urine specimens from enterobacterial UTI was 87-99%. In contrast, the urine specimens of UTI by Pseudomonas aeruginosa were positive in fewer than 20% with anti-E. coli sera, but were positive in more than 85% in tests with antiserum to P. aeruginosa. The possible diagnostic application of the described tests was discussed.
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PMID:Detection of antigens from gram-negative bacilli in urine of children with urinary tract infections. II. Thermostable bacterial proteins. 265 35

The sera of 19 patients with a febrile disease of undetermined etiology were positive in the indirect immunofluorescence assay (IFA) to Legionella bozemanii serogroup 1 (Lb) and Rickettsia typhi (Rt). To both antigens, high titers of IgG-class and IgM-class antibodies were demonstrated. Several of the patients also had positive IFA and Weil-Felix reactions to Proteus vulgaris OX19 (PX 19). A sharp reduction of the serotiters to all three antigens was achieved by absorption of the sera with any one of the organisms. We demonstrated, by crossed immunoelectrophoresis with an Lb extract and a rabbit reference anti-Lb serum, that a heat-stable and trypsin-resistant antigen (antigen no. 1) reacted consistently with patients' sera that had been incorporated into an intermediate gel. Sera from five patients with high-titer IFA reactions to Rt, but no reaction to Lb, showed no interaction with antigen no. 1.
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PMID:Serological cross-reactions between Rickettsia typhi, Proteus vulgaris OX19, and Legionella bozemanii in a series of febrile patients. 309 99

The purified RecA proteins encoded by the cloned genes from Proteus vulgaris, Erwinia carotovora, Shigella flexneri, and Escherichia coli B/r were compared with the RecA protein from E. coli K-12. Each of the proteins hydrolyzed ATP in the presence of single-stranded DNA, and each was covalently modified with the photoaffinity ATP analog 8-azidoadenosine 5'-triphosphate (8N3ATP). Two-dimensional tryptic maps of the four heterologous RecA proteins demonstrated considerable structural conservation among these bacterial genera. Moreover, when the [alpha-32P]8N3ATP-modified proteins were digested with trypsin and analyzed by high-performance liquid chromatography, a single peak of radioactivity was detected in each of the digests and these peptides eluted identically with the tryptic peptide T31 of the E. coli K-12 RecA protein, which was the unique site of 8N3ATP photolabeling. Each of the heterologous recA genes hybridized to oligonucleotide probes derived from the ATP-binding domain sequence of the E. coli K-12 gene. These last results demonstrate that the ATP-binding domain of the RecA protein has been strongly conserved for greater than 10(7) years.
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PMID:Conservation of an ATP-binding domain among RecA proteins from Proteus vulgaris, Erwinia carotovora, Shigella flexneri, and Escherichia coli K-12 and B/r. 328 5

Sodium deoxycholate is used in a number of bacteriological media for the isolation and classification of gram-negative bacteria from food and the environment. Initial experiments to study the effect of deoxycholate on the growth parameters of Escherichia coli showed an increase in the lag time constant and generation time and a decrease in the growth rate constant and total cell yield of this microorganism. Cell fractionation studies indicated that sodium deoxycholate at levels used in bacteriological media interferes with the incorporation of [U-14C]glucose into the cold-trichloroacetic acid-soluble, ethanol-soluble, and trypsin-soluble cellular fractions of E. coli. Finally, sodium deoxycholate interfered with the flagellation and motility of Proteus mirabilis and E. coli. It would appear then that further improvement of the deoxycholate medium may be in order.
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PMID:The action of sodium deoxycholate on Escherichia coli. 331 Aug 88

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
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PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42


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