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At least 775 records · Page 43Linked to original sources
PubMed1987

Bacteriological studies of excess activated sludge subjected to aerobic mineralization.

Quantitative and qualitative changes in the composition of bacterial microflora occur in the course of mineralization of excess activated sludge formed during the purification of crude oil refining wastewaters were studied. The excess activated sludge was dominated by Gram-negative bacteria belonging to the genera Pseudomonas III and IV. Mineralization of the excess sludge in both stationary and semicontinuous systems was accompanied by quantitative changes in the composition of the individual groups of Gram-negative bacteria. The frequency of Pseudomonas was reduced in favour of the Enterobacteriaceae, Achromobacter and Alcaligenes.

Alcaligenes↗
PubMed1989

Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies.

The predicted cytoplasmic orientation and two-domain structure of the multidrug efflux pump P-glycoprotein were demonstrated with sequence-specific antibodies. We synthesized peptides corresponding to amino acid residues, Glu393-Lys408 (anti-P) and Leu1206-Thr1226 (anti-C) in P-glycoprotein from human mdr1 cDNA and used these peptides to produce polyclonal antibodies. From the primary structure of P-glycoprotein, and anti-C antibody is expected to recognize another position, Leu561-Thr581, in the duplicate structure of P-glycoprotein, but anti-P recognizes only one site. These antibodies bind to multidrug-resistant cells (KB-C2) with permeabilized plasma membrane but do not bind to nonpermeabilized KB-C2 cells or parental KB cells, supporting the predicted cytoplasmic orientation of these sequences. With immunoblotting of the membrane fractions from KB-C2 cells, a major 140-kDa polypeptide of the P-glycoprotein was detected with both anti-P and anti-C. Two minor polypeptides with molecular mass of 95 and 55 kDa were also detected. When membrane vesicles were digested mildly with trypsin, the amount of these two polypeptides increased. Anti-P detected only the 95-kDa polypeptide, and anti-C detected both 95- and 55-kDa polypeptides. Achromobacter lyticus protease I (lysyl endopeptidase) and Staphylococcus aureus V8 protease also produced two polypeptides with similar molecular weights. Absorption into lectin-agarose beads and labeling with [3H]glucosamine indicated that the 95-kDa polypeptide was glycosylated but that the 55-kDa polypeptide was not. These two polypeptides as well as P-glycoprotein were photoaffinity-labeled with a calcium channel blocker, [3H]azidopine, but most of the label was found in the 55-kDa polypeptide. The yield of labeled fragments from membrane vesicles photolabeled after digestion with trypsin was similar to that from membrane vesicles digested with trypsin after photolabeling. These data indicate 1) that the 95-kDa polypeptide is the fragment corresponding to the amino-terminal half of P-glycoprotein containing sugar chains; 2) that the 55-kDa polypeptide is the carboxyl-terminal half which was mainly labeled with [3H]azidopine; and 3) that P-glycoprotein has a relatively rigid structure with a small number of protease-sensitive sites and its global structure is not destroyed by tryptic cleavage.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMedDate not supplied

[Identification of non-fermenting gram-negative bacteria. "Havana Center" Pediatric Teaching Hospital. December 1986 through May 1987].

A study is made of non-fermenting gram-negative bacterial strains isolated at the Microbiology Lab, "Centro Habana" Pediatric Teaching Hospital. The strains studied come from various types of samples with prevalence of exudates and smears. A definite biotyping of 100% of strains is made. 90.0% are classified within the genus Pseudomonas. In addition, organisms of the genera Acinetobacter, Alcaligenes, Achromobacter, and Moraxella are identified. The most frequent species turned out to be Pseudomonas aeruginosa, which accounted for 68.4% of the total.

Bacterial Typing Techniques↗
PubMed1989

[Catalytic component of calmodulin-independent adenylate cyclase from bovine brain. Isolation and determination of partial amino acid sequence].

The catalytic component of calmodulin-independent adenylate cyclase of cattle cerebral cortex was solubilized and purified to the homogeneous state. The conditions for preparative obtaining of the enzyme on the column with immobilized antibodies to adenylate cyclase were found. These antibodies were proved to interact with the calmodulin-independent rather than the calmodulin-dependent form of the enzyme. Molecular mass of the calmodulin-independent adenylate cyclase determined electrophoretically is 140 +/- 10 kDa. Amino acid composition of the enzyme and sequences of its fragments (in total 300 amino acid residues) obtained upon treatment with lysyl-specific proteinase from Achromobacter liticus were determined. Clone containing a cDNA 605 bp insertion coding for the 183 amino acid residue fragment of adenylate cyclase was isolated from the bovine brain cDNA library. Homology of this fragment to the known sequences of Escherichia coli and Bordetella pertussis adenylate cyclases was revealed.

Adenylyl Cyclases↗
PubMed1989

Determination of partial amino acid sequence of lipoate acetyltransferase of rat pyruvate dehydrogenase complex.

The partial amino acid sequence of rat lipoate acetyltransferase was determined using the intact protein and the peptides derived from a digest with Achromobacter protease I. The results showed the amino-terminal sequence of the mature enzyme to be (N) Ser-Leu-Pro-Pro-His-Gln-Lys-Val-Pro-Leu-Pro-Ser- Leu-Ser-Pro-Thr-Met-Gln-Ala-Gly-Thr-Ile-Ala-Arg-Trp-Glu-Lys. In addition, the sequences of two possible lipoyl-binding sites in the subunit, which are very similar to each other, were established.

Acetyltransferases↗
PubMed1989

[Production of antibiotic substances by natural variants of the marine bacterium Vibrio Fischeri].

It was shown that under definite conditions there was competition between natural variants of sea bacteria belonging to V. fischeri. Natural variants of V. fischeri, strain 6 differed in their resistance to streptomycin and had different growth rates under conditions of limited aeration. Morphologically all the variants were identical. V. fischeri P-0, V. fischeri P-1 and V. fischeri P-2 were studied. The study revealed that V. fischeri P-0 produced a non-dialysing thermostable trypsin-sensitive substance inhibiting the growth of V. fischeri P-1 and V. fischeri P-2. The maximum activity of the antibacterial substance was observed when V. fischeri P-0 was grown in a liquid medium with peptone and yeast extract without agitation at 26 degrees C. The inhibiting substance was also active against V. fischeri BKM B995 and V. fischeri P-7 isolated as a result of V. fischeri P-0 exposure to ethidium bromide. The substance had no effect on the following bacterial species: Aeromonas liquefaciens 301, Achromobacter liquefaciens, Pseudomonas putida 15, Pseudomonas fluorescence 7, Escherichia coli AH-32 and Staphylococcus aureus.

Anti-Bacterial Agents↗
PubMed1988

Complete amino acid sequence of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

The complete amino acid sequence of 6-phospho-fructo-2-kinase/fructose-2,6-bisphosphatase from rat liver was determined by direct analysis of the S-carboxamidomethyl protein. A complete set of nonoverlapping peptides was produced by cleavage with a combination of cyanogen bromide and specific proteolytic enzymes. The active enzyme is a dimer of two identical polypeptide chains composed of 470 amino acids each. The NH2-terminal amino acid residue of the polypeptide chain was shown to be N-acetylserine by fast atom bombardment mass spectrometry of the purified N-terminal tetradecapeptide isolated after cleavage of the intact S-carboxamidomethylated protein with lysyl endoproteinase (Achromobacter protease I). Alignment of the set of unique peptides was accomplished by the analysis of selected overlapping peptides generated by proteolytic cleavage of the intact protein and the larger purified cyanogen bromide peptides with trypsin, Staphylococcus aureus V8 protease, and lysyl endoproteinase. Four nonoverlapping peptides were aligned by comparison with the amino acid sequence predicted from a partial cDNA clone encoding amino acid positions 166-470 of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (Colosia, A.D., Lively, M., El-Maghrabi, M. R., and Pilkis, S. J. (1987) Biochem. Biophys. Res. Commun. 143, 1092-1098). The nucleotide sequence of the cDNA corroborated the peptide sequence determined by direct methods. A search of the Protein Identification Resource protein sequence database revealed that the overall amino acid sequence appears to be unique since no obviously homologous sequences were identified. However, a 100-residue segment of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (residues 250-349), including the active site histidine residue of the bisphosphatase domain, was found to be homologous to the active site regions of yeast phosphoglycerate mutase and human bisphosphoglycerate mutase.

Amino Acid Sequence↗
PubMed1988

Characterization of the major protein-tyrosine-phosphatases of human placenta.

In the preceding article (Tonks, N. K., Diltz, C. D., and Fischer, E. H. (1988) J. Biol. Chem. 263, 6722-6730), the purification of the major protein-tyrosine-phosphatases from human placenta, some to apparent homogeneity, was described. This report compares the characteristics of these enzymes and clearly identifies at least two distinct protein-tyrosine-phosphatase catalytic subunits. All were absolutely specific for phosphotyrosyl residues and showed no activity on any of the phosphoseryl/phosphothreonyl-containing proteins tested; they exhibited a high affinity for substrate with Km values in the submicromolar range. All were absolutely dependent on sulfhydryl compounds and appeared to contain at least one highly reactive cysteinyl residue essential for activity. Subtypes 1A and 1B could be distinguished by their response to polyanionic and polycationic compounds. The 1B enzymes were activated by EDTA, spermine, spermidine, and myelin basic protein to a greater extent than the 1A subtypes. Furthermore, they were inhibited by approximately 2 orders of magnitude lower concentrations of heparin (IC50 approximately 20 nM) and 1:1 or 4:1 poly (glutamate/tyrosine) (IC50 approximately 50 nM) than the 1A subtypes. Surprisingly, inhibition by the glutamate/tyrosine copolymers was strictly noncompetitive. Peptide mapping following digestion with Achromobacter protease I or Staphylococcus aureus V8 protease supported the view that, whereas protein-tyrosine-phosphatase subtypes 1A and 1B are different, their soluble and particulate counterparts are closely related structurally and are distinct from serine/threonine phosphatases 1 and 2A.

Chromatography, High Pressure Liquid↗
PubMed1988

Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence.

The complete amino acid sequence of acetyl-CoA carboxylase from chicken liver has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA. The results were confirmed by Edman degradation of peptide fragments obtained by digestion of the enzyme polypeptide with Achromobacter proteinase I or staphylococcal serine proteinase. Chicken liver acetyl-CoA carboxylase is predicted to be composed of 2,324 amino acid residues, having a calculated molecular weight of 262,706. The biotin carboxyl carrier protein domain is located in the middle region of the enzyme polypeptide. The amino-terminal portion of the acetyl-CoA carboxylase has been found to exhibit a homologous primary structure to that of carbamyl phosphate synthetase. Localization of possible functional domains including biotin carboxylase subsite in the acetyl-CoA carboxylase polypeptide is discussed.

Acetyl-CoA Carboxylase↗
PubMed1986

[Peptide inhibitors of a bacterial collagenase].

The properties of the cleavage site of collagen by collagenases remain discussed. The authors report their studies on the active site of the collagenase of a bacteria, achromobacter, based on two types of methods. The first type uses synthetic substrates, the second one enzymatic inhibitors. The results of both methods are reviewed. The inhibitors seem more sensitive than substrates to study the relation between structure and activity of the enzyme.

Alcaligenes↗
PubMed1988

A phospholipase A2 in the supernatant fraction of rat spleen. Its similarity to rat pancreatic phospholipase A2.

Rat spleen supernatant contained two forms of calcium-dependent cellular phospholipase A2 which could be separated from each other by TEAE-cellulose chromatography. The phospholipase A2, named PLA2 S-1, present in the major flow-through fraction was purified to homogeneity. The structural and catalytic properties of splenic PLA2 S-1 were systematically compared with those of rat pancreatic phospholipase A2. Structural evidence, including the sequence of the N-terminal 32 residues, peptide maps obtained on Achromobacter protease I digestion and cyanogen bromide cleavage, and the amino acid composition, showed the close similarity of the two enzymes. Their catalytic and immunochemical properties were also similar. These results demonstrated the existence of a pancreatic type phospholipase A2 in a non-pancreatic organ as a member of the cellular phospholipases A2 and suggest the potential functional involvement of pancreatic type phospholipase A2 in cellular phospholipid metabolism.

Amino Acid Sequence↗
PubMed1987

[Treatment of post-traumatic and post-neurosurgical bacterial meningitis with ceftriaxone alone or in combination with fosfomycin].

From 1984 to 1986, 13 patients (10 adults, 3 children) with bacterial meningitis following neurosurgery or traumatism were given ceftriaxone alone 6 times at a dose of 40 mg/kg one IV injection per day, or in association 7 times with fosfomycin at a dose of 200 mg/kg/day, 3 IV perfusions every 4 h. The bacteriological diagnosis was confirmed in 9 cases (3 Staphylococcus aureus, 4 Streptococcus pneumoniae, 1 Klebsiella, 1 Peptococcus). In vitro neither synergy nor antagonism were observed between the two antimicrobial agents. The acute infections episode resolved in all patients except on who died with a negative CSF culture. One superinfection meningitis with Achromobacter was seen. CSF concentrations of ceftriaxone were assayed and found to be comparable with those reported by most authors. Tolerance was excellent for all our patients.

Adult↗
PubMed1988

Trapping of nitric oxide produced during denitrification by extracellular hemoglobin.

A spectrophotometric method has been developed that uses extracellular hemoglobin (Hb) to trap nitric oxide (NO) released during denitrification as nitrosyl hemoglobin (HbNO). The rate of complexation of NO with Hb is about at the diffusion controlled limit for protein molecules and the product, HbNO, is essentially stable. Hb was added to an anaerobic bacterial suspension and denitrification was initiated with either KNO2 or KNO3. HbNO formation was observed for six species of denitrifying bacteria and showed isosbestic points at 544, 568, and 586 nm. Cellular NO production, presumably by nitrite reductase, was kinetically distinct from the much slower chemical reaction of Hb with KNO2 to form methemoglobin and HbNO. The rate of HbNO formation was proportional to cell density, essentially independent of pH from 6.8 to 7.4, nearly zero order in [Hb] and, at least with Paracoccus denitrificans, strongly inhibited by rotenone and antimycin A. The Cu chelator, diethyldithiocarbamate, had no effect on HbNO formation by Pa. denitrificans, but abolished that by Achromobacter cycloclastes which uses a Cu-containing nitrite reductase known to be inactivated by the chelator. HbNO formation did not occur with non-denitrifying bacteria. The stoichiometry at high [Hb] for conversion of Hb to HbNO was 1.3-1.8 KNO2 per Hb for Pa. denitrificans, Pseudomonas aeruginosa, and A. cycloclastes and about 3.4 for Pseudomonas stutzeri. The former range of values corresponds to a partition of about 2 N atoms in 3 toward trapping and 1 in 3 toward reduction on the pathway to N2. Nitrogen not trapped appeared largely as N2O in presence of acetylene. The results are consistent with a model in which NO is a freely diffusible intermediate between nitrite and N2O, providing that nitric oxide reductase is or nearly is a diffusion controlled enzyme.

Antimycin A↗
PubMed1978

[In vitro activity of cefoxitin compared with the activity of other antibiotics and trimethoprim-sulfamethoxazole (author's transl)].

The new developed antibiotic cefoxitin has been tested in vitro on its effectiveness against bacteria isolated from human material. Pseudomonas aeruginosa and streptococci of the serological group D were not tested, because these microorganisms are not sensitive against this antibiotic. Besides cefoxitin other antibiotics (cephalothin, cephalexin, ampicillin, carbenicillin, tetracycline, gentamicin, penicillin G, oxacillin) and trimethoprim-sulfamethoxazole were also tested. As to the results cefoxitin shows the best effectiveness against all gram-positive bacteria and against gram-negative bacteria including indol-positive species of proteus, providencia, serratia marcescens and the anaerobe, gram-negative, non-spore-forming rods. There are different results with enterobacter-, citrobacter-, achromobacter- and acinetobacter-species.

Anti-Bacterial Agents↗
PubMed1986

[Application of a micromethod to the study of the bactericidal activity of 2 antiseptics based on chlorhexidine gluconate].

Minimal bactericidal concentrations (MBCs) of two antiseptics containing chlorhexidine digluconate (5% for the A solution, 1.5% for the B solution) were determined using a microdilution method. This method is a miniaturization of the Afnor T 72150 standard for antiseptics and disinfectants. 133 hospital isolates were studied, including 68 Enterobacteriaceae, 11 Acinetobacter, 18 Pseudomonas, 1 Achromobacter, 23 Staphylococcus, and 12 S. faecalis. Each microplate was seeded with eleven of these strains and one reference strain (E. coli CIP 54127, P. aeruginosa CIP A22, S. aureus CIP 53154, and S. faecium CIP 5855). Ten microliter of a standardized inoculum (2 to 3 10(8) bacteria/ml) were added to 90 microliters of a solution containing the antiseptic. Each antiseptic was tested in various concentrations (1.95 to 125 mg/l for A and 1.17 to 75 mg/l for B). After five minutes contact at 21 degrees C, 1.5 microliter from each well was seeded on a neutralizing agar plate (letheen agar + 3% tween 80 + 0.3% lecithin + 3% saponin + 0.1% histidine). The neutralizing effectiveness of this plate on the antiseptics in the concentrations used had been ascertained previously. The Afnor T 72150 standard was established for each reference strain. MBCs 90 (in mg/l) found were as follows: 31.2 (A) and 18.8 (B) for Enterobacteriaceae, 15.6 (A) and 9.4 (B) for Acinetobacter, 31.2 (A) and 18.8 (B) for Pseudomonas, 62.5 (A) and 37.7 (B) for Staphylococcus and 125 (A) and 37.5 (B) for S. faecalis.(ABSTRACT TRUNCATED AT 250 WORDS)

Anti-Infective Agents, Local↗
PubMed1986

[Amino acid metabolism by thin layer chromatography for the differentiation of Bordetella and Alcaligenes species].

The amino acid metabolism of Bordetella and Alcaligenes strains was investigated for differentiation purposes. All species investigated reacted differently with a number of amino acids. The genus Bordetella could be differentiated from that of Alcaligenes by its inability to metabolize L-lysine, L-arginine and D-histidine. The recently described species Bordetella avium, as well as Achromobacter xylosoxidans (Yabuuchi), considered as Alcaligenes denitrificans subsp. xylosoxidans, presented themselves as independent species too. Bordetella odorans, now assigned to the species Alcaligenes faecalis was indistinguishable from the other strains of Alcaligenes faecalis investigated.

Alcaligenes↗
PubMed1987

Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa.

The glycoprotein (GP) IIb-IIIa complex was isolated from human platelet membranes by immunoaffinity chromatography using a monoclonal antibody specific for GP IIb-IIIa. GP IIb and IIIa were further separated in the presence of sodium dodecyl sulfate (SDS) by gel filtration high-performance liquid chromatography (HPLC). Two cycles of this procedure yielded almost complete separation of homogeneous preparations of GP IIb and IIIa. Each protein was then digested with lysyl endopeptidase (Achromobacter protease I), which cleaves at the carboxyl side of lysine residues, and the resulting oligopeptides from GP IIb and IIIa were fractionated with HPLC using a C18 reverse-phase column. Comparison of the elution profiles showed no obvious homology between the two proteins. Amino acid sequences of selected oligopeptides from each glycoprotein were determined using a gas-phase protein sequencer. Sixty amino acid residues (26 residues for IIb and 34 residues for IIIa) were identified.

Amino Acid Sequence↗