Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Since 1973 30 patients with urinary tract infections (UTI) or pyelonephritis have been treated with sisomicin, a new aminoglycoside, in a daily dose of 2 mg/kg for a period of seven to nine days. From a clinical point of view the result of treatment was good. Complete resolution was achieved in 17 patients, improvement in nine, and there was no effect in four patients. Thirty-five causative organisms (Escherichia coli = 23, Proteus sp. = 7, Klebsiella sp. = 3, Pseudomonas aeruginosa = 1, Citrobacter = 1) were isolated before treatment. Thirty of the organisms were eliminated during treatment, but seven reappeared during the follow-up period; five strains persisted. Side effects observed consisted of reversible increase of serum creatinine in four patients, excretion of granular casts in 14 patients, and a transient rise of alkaline phosphatase, SGOT and/or SGPT in five patients. No signs of ototoxicity or any other adverse reactions were found and local tolerance was good. In 20 patients blood samples for assay were obtained daily one hour after i. m. injection of 1.0 mg/kg. No evidence of drug accumulation in the serum was found: the mean serum concentrations one hour after injection remained between 3.4 and 3,9 microgram/ml during the entire treatment period. Sisomicin is a highly effective antibiotic for the treatment of UTI caused by gramnegative pathogens. On account of its potential toxicity however, it should be used, like other aminoglycosides, only in selected cases.
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PMID:[Efficacy, tolerance, and pharmacokinetics of sisomicin in urinary tract infections (author's transl)]. 10 44

We report the development and testing of an enzyme-linked immunosorbent assay with excellent sensitivity for the detection of Haemophilus influenzae type b (HI(b)) antigen in clinical specimens from patients with HI(b) meningitis. The assay, an indirect sandwich technique, uses polystyrene balls as a solid phase and an alkaline phosphatase-labeled goat anti-rabbit globulin conjugate. Specimens are incubated with polystyrene balls armed with burro anti-HI(b) antiserum, and recognition antibody is visualized by addition of alkaline phosphatase-labeled anti-globulin, together with the enzyme substrate p-nitrophenyl phosphate. Concentrations of antigen are determined from standard curves prepared by using purified HI(b) capsular antigen polyribophosphate. The assay reproducibly detects polyribophosphate at concentrations between 1 and 5 ng/ml. Cross-reactions have not as yet been encountered in simulated and authentic clinical specimens containing other species including Escherichia coli, Klebsiella pneumoniae, group B Streptococcus, Pseudomonas aeruginosa, Streptococcus pneumoniae, Staphylococcus aureus, Neisseria meningitidis, and Listeria monocytogenes. In preliminary tests with 11 spinal fluid specimens, 2 serum specimens, and 5 urine specimens from patients with culture-proved HI(b) meningitis, antigen was detected in all specimens in concentrations ranging from 1 to 7,000 ng/ml. Antigen was not detected in any of 62 clinical specimens which were culture negative for HI(b), including 11 spinal fluid specimens from patients with bacterial meningitis caused by microorganisms other than HI(b). The enzyme-linked immunosorbent assay technique described here is considerably simpler than radioimmunoassay and, based on concurrent tests with 14 positive clinical specimens, may be more sensitive than counterimmunoelectrophoresis. It seems, therefore, to hold considerable promise for clinical use in rapid detection of systemic HI(b) infections.
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PMID:Indirect sandwich enzyme-linked immunosorbent assay for rapid detection of Haemophilus influenzae type b infection. 39 14

Basic and clinical investigation on the intravenous administration of sulbenicillin in moderate dose (510g daily) was carried out to evaluate its clinical effect in systemic infections due to gram-negative bacilli. The following results were obtained. (1) In human subjects received 5 g intravenous drip infusion, the peak blood levels were found at the end of infusion. In 6 cases with normal renal function (Ccr greater than or equal to 70ml/min.) the peak blood level was 181 mcg/ml on the average and the half-life 1.1 hours, while in 3 cases with impaired renal function (Ccr less than 70 ml/min.) the peak level 216 mcg/ml and the half-life longer than 2 hours. The height of the peak level seemed to be subjected to the duration of infusion. The renal excretion of sulbenicllin was 55.2% on the average both in cases with normal and impaired renal functions. (2) Sulbenicillin, 510g daily divided in 2 doses, was administered to 15 cases including 6 cases with acute pyelonephritis, 3 with acute cystitis, 3 with biliary tract infection, 2 with respiratory tract infection and 1 with acute prostatitis. All the cases except 3 cases with acute pyelonephritis had underlying diseases. Escherichia coli was isolated from 10 cases, Klebsiella from 2, Pseudomonas aeruginosa from 1, and unidentified gram-negative bacilli from 1. Eleven cases responded to the treatment, but 4 cases failed. In 11 cases with susceptible bacteria, 8 cases responded bacteriologically (2 cases recurred), and 3 cases failed to respond. A case with biliary tract infection due to E. coli did not respond to 5 g daily treatment, but responded to 5 g twice daily. Two cases due to organisms which were not inhibited by 200mcg/ml in vitro did not respond to the treatment. (3) A moderate decrease in red blood cell number and hemoglobin content was observed in one case. A transient increase in transaminase and alkaline phosphatase level was observed in other cases.
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PMID:[Studies on the intravenous administration of sulbenicillin (author's transl)]. 77 28

Transfer of the IncN group plasmid pCU1 from Escherichia coli to Klebsiella oxytoca by conjugation kills a large proportion (90 to 95%) of the recipients of plasmid DNA, whereas transfer to E. coli or even to the closely related Enterobacter aerogenes does not. Two regions, kikA and kikB, have been identified on pCU1 that contribute to the Kik (killing in klebsiellas) phenotype. We have localized the kikA region to 500 bp by deletion analysis and show by DNA-DNA hybridization that kikA is highly conserved among the plasmids of incompatibility group N. The expression in K. oxytoca of kikA under the control of the strong inducible E. coli tac promoter results in loss of cell viability. The nucleotide sequence showed two overlapping open reading frames (ORFs) within the kikA region. The first ORF codes for a putative polypeptide of 104 amino acids (ORF104). The second ORF codes for a 70-amino-acid polypeptide (ORF70). The properties of the putative protein encoded by ORF104 and gene fusions of kikA to alkaline phosphatase by using TnphoA suggest that killing may involve an association with the bacterial membrane; however, we could not rule out the possibility that ORF70 plays a role in the Kik phenotype.
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PMID:Isolation and characterization of kikA, a region on IncN group plasmids that determines killing of Klebsiella oxytoca. 156 33

The authors report a nonradioactive adaptation of DNA hybridization technology for the direct detection of Legionella organisms in situ in routinely processed histologic specimens. The probe used consisted of synthetic oligodeoxynucleotides, complementary to the ribosomal RNA of all clinically relevant Legionella species, labeled with biotinylated dUTP at their 3' ends. By in situ DNA hybridization and detection with an avidin-alkaline phosphatase complex. Legionella was visualized by light microscopy within the alveoli of lung specimens in 9 of 13 direct fluorescent antibody- or culture-positive cases of Legionnaires' disease. No cross-hybridization was observed in lung specimens infected with Pseudomonas aeruginosa, Klebsiella pneumoniae, Streptococcus pneumoniae, or other pathogens. The authors' results illustrate a novel adaptation of in situ DNA hybridization techniques, usually used for viruses, to the detection of a bacterial organism. The method enables direct visualization of bacterial nucleic acid in infected tissues and may facilitate early diagnosis and treatment of legionellosis.
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PMID:Rapid diagnosis of Legionella infection by a nonisotopic in situ hybridization method. 202 27

The determined nucleotide sequence of the Klebsiella pneumoniae UNF5023 gene pulA comprises a single open reading frame coding for a 1090-residue precursor of the secreted protein pullulanase. The predicted sequence of this protein is highly homologous to that of pullulanase of Klebsiella aerogenes strain W70. However, the UNF5023 pullulanase lacks a collagen-like sequence present at the N-terminus of the mature W70 enzyme and differs further from the W70 pullulanase around residue 300 and at the C-terminus. Pullulanases with or without the collagen-like sequence could not be separated by gel electrophoresis under denaturing or non-denaturing conditions, and were unaffected by collagenase. A large central domain which is highly conserved in both UNF5023 and W70 polypeptides contains eight short sequences that are also found in amylases and iso-amylases. Linker mutations in the region of the UNF5023 pulA gene coding for this domain abolished catalytic activity without affecting transport of the polypeptide across the outer membrane. Hybrid proteins comprising at least the amino-terminal 656 residues of prepullulanase fused to alkaline phosphatase were partially localized to the cell surface, as judged by their accessibility to anti-pullulanase serum in immuno-fluorescence tests. On the basis of these results, we tentatively propose that secretion signals required for recognition and translocation across the outer membrane via the pullulanase-specific extension of the secretion pathway are located near the N-terminus of the pullulanase polypeptide.
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PMID:Molecular characterization of pulA and its product, pullulanase, a secreted enzyme of Klebsiella pneumoniae UNF5023. 218 Dec 42

The structure and function of the phoB and phoR genes of Shigella dysenteriae strains and Klebsiella pneumoniae, which are involved in regulation of the phosphate regulon, were analyzed. Complementation tests among the genes of Escherichia coli, S. dysenteriae strains, and K. pneumoniae for production of alkaline phosphatase indicate that S. dysenteriae serotype 2 and serotype 3 strains and K. pneumoniae are phoA+ phoB+ phoR+ but S. dysenteriae Sh and serotype 1 strains are phoA phoB+ phoR. Nucleotide sequences of phoB and phoR of S. dysenteriae Sh and K. pneumoniae are highly homologous to those of E. coli, except for a single base insertion found in phoR of S. dysenteriae Sh.
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PMID:Phosphate regulon in members of the family Enterobacteriaceae: comparison of the phoB-phoR operons of Escherichia coli, Shigella dysenteriae, and Klebsiella pneumoniae. 255 68

This investigation was initiated as a consequence of several cases of diarrhea in a nursery ward for preterm babies in Nairobi, Kenya. Ten lactose-positive colonies were isolated from the stools of each of 30 neonates, regardless of whether they had diarrhea; 229 strains were identified as Escherichia coli and 65 strains were identified as Klebsiella pneumoniae. Six strains were lost during laboratory handling. No other bacterial, viral, or parasitic enteropathogens were identified. Using synthetic alkaline phosphatase-labeled probes, the bacterial isolates were found to be negative for the presence of genes coding for heat-stable and heat-labile enterotoxins. Seventy-eight E. coli strains isolated from a total of 13 neonates possessed the E. coli enteropathogenic adhesion factor (EAF) gene, as demonstrated by the use of a cloned radiolabeled DNA fragment probe. These strains possessed similar plasmid profiles constituting a core plasmid profile, and while all adhered to HeLa cells, none produced Vero cell cytotoxins. The EAF gene was located on a 65-megadalton plasmid. Serotyping showed the strains to be of serogroup O111 and serotype H nontypable, a well known enteropathogenic type. Five neonates died during the outbreak, and the fatality rate was 30.7% (4 of 13) for neonates infected with EAF-positive E. coli strains compared with 7.7% (1 of 13) for neonates from whom only EAF-negative E. coli strains were isolated. K. pneumoniae only was isolated from five neonates.
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PMID:Enteropathogenic Escherichia coli serotype O111:HNT isolated from preterm neonates in Nairobi, Kenya. 256 96

A specific monoclonal antibody for Escherichia coli and Shigella sp. alkaline phosphatase was used in an immunocapture assay and allowed identification of E. coli either in culture isolates or directly in clinical specimens. The assay was easy and required only four steps: (i) alkaline phosphatase was released within 10 min by using a gentle lysis procedure, (ii) cell lysates were transferred to antibody-coated tubes for 45 min, (iii) p-nitrophenyl phosphate substrate was added, and (iv) alkaline phosphatase activity was detected in a microsample spectrophotometer at 410 nm. This immunocapture assay was highly specific: only one false-positive reaction was observed with a Klebsiella pneumoniae lysate among the 205 non-E. coli strains tested. The assay was sensitive, detecting 10(7) CFU/ml from culture isolates or 10(5) CFU/ml from urine specimens which had first been grown in phosphate-limiting medium for 2 h. At these bacterial concentrations, the percentages of detected E. coli were high: 91% for blood cultures, 95.4% for culture isolates, and 96.8% for urine specimens.
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PMID:Alkaline phosphatase capture test for the rapid identification of Escherichia coli and Shigella species based on a specific monoclonal antibody. 267 Oct 16

A series of fusions between the gene for the Klebsiella pneumoniae secreted lipoprotein pullulanase (pulA) and the genes for cytoplasmic beta-galactosidase (lacZ) or periplasmic alkaline phosphatase (phoA) were created by transposon mutagenesis using mini-MudII1681 or TnphoA, respectively. The hybrid genes were expressed in Escherichia coli K-12 with or without the K. pneumoniae genes that promote pullulanase secretion in E. coli. We characterized seven different pulA-lacZ gene fusions encoding hybrid polypeptides containing from 14 to c. 1060 residues of pro-pullulanase. All but the smallest hybrid were fatty acylated and were toxic to producing cells, causing the accumulation of precursors of other exported proteins. Four different pulA-phoA gene fusions encoded hybrids with alkaline phosphatase activity. All four hybrids were fatty acylated, but were not toxic. Although the hybrids were apparently membrane-associated, they were not secreted into the medium either by E. coli carrying pullulanase secretion genes or by K. pneumoniae. Immunofluorescence tests indicated that the pullulanase secretion genes promoted the localization of one of these hybrids to the outer face of the E. coli outer membrane, which may have important implications for the design of live vaccine strains and of immobilized enzymes.
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PMID:A gene fusion approach to the study of pullulanase export and secretion in Escherichia coli. 332 97


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