Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026918 (Mycobacterium)
 52,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lymph nodes from guinea pigs inoculated with Mycobacterium tuberculosis were fixed in buffered formalin, then treated for the recommended times in Gooding and Stewart's fluid, EDTA, aqueous nitric acid, von Ebner's fluid, and rapid decalcifier (RDC). The blocks were processed to paraffin wax and sections were stained by the Ziehl-Neelsen technique. Only in sections of the blocks treated with RDC were no acid alcohol fast bacilli demonstrable. Hydrochloric acid is a known constituent of RDC and it was found that Myco. tuberculosis is altered by treatment with 2-5M solutions of hydrochloric acid and above and cannot subseuqently be demonstrated by the Ziehl-Neelsen stain. From these results it is recommended that calcified tissue from patients in whom there is a suspicion of tuberculosis should be decalcified with an agent other than RDC.
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PMID:Effect of decalcifying agents on the staining of Mycobacterium tuberculosis. 5 59

Fatty acid synthetase from Mycobacterium smegmatis has been purified to near homogeneity as judged by a variety of electrophoretic criteria under both native and dissociating conditions. A single protein band was obtained on gel electrophoresis in sodium dodecyl sulfate or 8 M urea at various pH values and on isoelectric focusing in 8 M urea. A subunit molecular weight of about 290,000 was found by polyacrylamide gel electrophoresis in sodium dodecyl sulfate or by sedimentation equilibrium ultracentrifugation in 6 M guanidine HCl. Quantitative Quantitative determination of pantetheine, of flavin, and of the number of fatty acids synthesized during a single enzyme turnover all yield values corresponding to a stoichiometry of about 1 mol per mol of subunit, providing strong evidence that M. smegmatis fatty acid synthetase is an oligomer of identical, multifunctional polypeptide chains.
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PMID:Subunit structure of Mycobacterium smegmatis fatty acid synthetase. Evidence for identical multifunctional polypeptide chains. 63 92

The 38-kDa protein (Ag38) of the Gram+ bacterium, Mycobacterium tuberculosis H37Rv, is an immunodominant antigen of potential utility for diagnosis and vaccine development. Assessment of this potential requires large amounts of the purified protein that would be difficult, if not impossible, to obtain from M. tuberculosis itself. The gene coding for Ag38 had been previously cloned and in the present study was expressed as an unfused protein in Escherichia coli under the control of strong transcriptional (bacteriophage lambda pLpR) and translational (atpE) signals. Fermentation of the recombinant E. coli K-12 strain CAG629[pMS9-2], which is deficient in Lon protease and the heat-shock response, produced recombinant Ag38 (reAg38) at high levels (about 10% of total cellular protein). The reAg38, which accumulated as inclusion bodies, was completely solubilized in 6 M guanidine.HCl, refolded and purified to apparent homogeneity. The product showed the expected amino acid composition and M(r), and had similar reactivities as the native protein with three different mAb. Polyclonal antibodies raised against reAg38 reacted strongly with the native antigen in enzyme-linked immunosorbent assay. These results demonstrate that reAg38, which cannot be distinguished antigenically from the native protein of M. tuberculosis, can be prepared in quantity from E. coli.
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PMID:The Mycobacterium tuberculosis 38-kDa antigen: overproduction in Escherichia coli, purification and characterization. 137 65

Some 2-benzylbenzimidazole and 2-phenoxymethylbenzimidazole derivatives were synthesized and tested for in vitro tuberculostatic activity against Mycobacterium tuberculosis H 37 Rv. and human type wild strain (protocol n degrees.4186). The synthesized compounds have one of the CH3, Cl, NO2 or OCH3 groups at position 5 and 4' and are prepared by heating appropriate o-phenylenediamines with the carboxylic acids in the presence of 4.5N HCl. The experiments indicate that 2-phenoxymethylbenzimidazoles were more active than the corresponding 2-benzylbenzimidazoles. The most active compound was 5-chloro-2-phenoxymethylbenzimidazole (IIc) (MIC: 125 micrograms/ml).
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PMID:In vitro tuberculostatic activities of some 2-benzylbenzimidazole and 2-phenoxymethylbenzimidazole derivatives. 251 3

Mycobacterium bovis ATCC No. 19210 was grown on Middlebrook 7H-10 medium with pyruvate. Cells were harvested, and extracts were prepared, using 2% sodium deoxycholate (DOC) and 0.003M EDTA (in 0.1M Tris-HCl, 0.15M NaCl with 0.02% sodium azide [pH 8.4]). Phenylmethylsulfonyl fluoride was added, and the cells were extracted for 48 hours at 4 C. Cells were removed by centrifugation at 10,000 X g for 30 minutes. The supernatant was filter sterilized and separated into 2 fractions (peak A and peak B) by size-exclusion chromatography. The nonfractionated DOC extract and DOC peak A elicited delayed-type hypersensitivity responses at each of the protein concentrations tested (0.5, 1.5, and 4.5 micrograms) in M bovis-sensitized guinea pigs; responses were not detected, using DOC peak B. Significant differences were detected for each of the antigens when enzyme-linked immunosorbent assay values were compared, using sera from cattle before and 10 months after they were exposed to M bovis (P less than 0.01).
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PMID:Use of sodium deoxycholate to extract cell wall components of virulent Mycobacterium bovis. 354 7

Extracts of Mycobacterium bovis ATCC 19210 were prepared from cells following treatment with acetone 3 times, ethyl alcohol-ether 3 times (1:1, v/v), and chloroform 3 times. Cells were dried and suspended in 0.05M Tris-HCl (pH 7.5) containing lysozyme (1 mg/50 mg of dried cells). One aliquot of the lysozyme extract was filter-sterilized and 1 aliquot of the lysozyme extract was autoclaved. Delayed-type hypersensitivity responses elicited in sensitized guinea pigs, using the filter-sterilized lysozyme extract, were significantly greater than responses elicited using the autoclaved lysozyme extract (P less than 0.01). The filter-sterilized lysozyme extract and a purified protein derivative (PPD) of M bovis, at equal protein concentrations, elicited comparable delayed-type hypersensitivity responses in sensitized guinea pigs. Significant differences were not detected between the mean enzyme-linked immunosorbent assay (ELISA) values on sera collected from calves before exposure to M bovis, using each of the lysozyme extracts or the M bovis PPD (P greater than 0.05). Significant differences were detected when ELISA values obtained using each of the antigens on post-exposure serum were compared with ELISA values on serum collected from calves before exposure to M bovis (P less than 0.01). Differences were not detected in mean ELISA values on sera from cattle collected 12 months after exposure to M bovis, using each of the lysozyme extracts or M bovis PPD (P greater than 0.05); however, 8 of 8 calves were identified as positive on ELISA, using the filter-sterilized lysozyme extract, 7 of 8 calves were positive, using M bovis PPD, and 7 of 8 calves were positive, using the autoclaved lysozyme extract.
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PMID:In vitro and in vivo evaluation of lysozyme extracts of virulent Mycobacterium bovis in guinea pigs and calves. 390 33

Tween 80-hydrolyzing esterases produced by various species of rapidly growing mycobacteria were partially purified from sonicated cell lysates by diethylaminoethyl (DEAE) cellulose and subsequent Sephadex G-150 column chromatographies. The amount of the esterase produced per gram of bacterial cells varied markedly with each species. Mycobacterium smegmatis, M. chelonei, and M. phlei were high producers and M. chitae and M. diernhoferi were low producers of Tween-hydrolyzing esterase. The resistance of each mycobacterial strain to oleic acid correlated well with their esterase-producing ability. All the esterases studied were adsorbed on DEAE cellulose in 50 mM Tris-HCl buffer (pH 7.5), indicating that they are acidic proteins. Esterases of M. smegmatis, M. chitae, M. fortuitum, and M. phlei were eluted from DEAE at high concentrations (0.11-0.18 M) of ammonium sulfate, while those of M. parafortuitum and M. diernhoferi were eluted at lower concentrations (0.05-0.08 M). With Sephadex G-150 gel filtration, all esterases were shown to have similar molecular weights (36,000 to 58,000). On the basis of heat-stability and trypsin- or chymotrypsin-sensitivity, these esterases were divided into three groups: one was heat-stable and protease-sensitive (M. smegmatis and M. fortuitum), another was heat-labile and protease-resistant (M. chelonei), and the other was the intermediate of the above two groups (M. diernhoferi).
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PMID:Physicochemical characterization of Tween 80-hydrolyzing esterases produced by rapidly growing mycobacteria. 664 84

The induction and passive transfer of interferons have been shown to depress the level of cytochrome P-450 drug metabolism system of liver microsomes. Inducers of alpha or beta (Type I) interferons, such as Tilorone-HCl, statalon, mengovirus and others, suppressed the cytochrome P-450 system of rats or mice after administration. Induction of gamma (Type II) interferon also resulted in depression of the cytochrome P-450 system of mice. The gamma interferon was induced by sensitization of mice with Mycobacterium bovis strain BCG followed by challenge with tuberculin. The degree of depression of the cytochrome P-450 system correlated with the levels of interferon induced. In addition, passive transfer of exogenous gamma interferon also resulted in depression of the murine cytochrome-450 system. The metabolism of diphenylhydantoin, a drug metabolized by cytochrome-450, was examined in mice in which gamma interferon was induced. The metabolism of diphenylhydanoin was severely inhibited in mice which interferon was induced, and the level of inhibition correlated with the titer of gamma interferon induced. Passive transfer of gamma interferon also depressed the metabolism of diphenylhydantoin by murine cytochrome P-450.
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PMID:Effects of interferon on drug metabolism. 681 39

Wall-deficient forms of Mycobacterium aurum were prepared by agitating the cells during exponential growth with D-cycloserine, glycine, lysozyme, EDTA and LiCl for approximately the time of three cell divisions (18 h). Wall-deficient forms were then converted to spheroplasts by gentle stirring with lysozyme and EDTA in a Tris/HCl buffer containing sucrose until all the cells appeared spherical by phase contrast microscopy. Subsequent lysis by nucleases followed by osmotic shock produced membrane vesicles. Ultrastructural and chemical properties of the spheroplasts and membrane vesicles are described. The spheroplasts were susceptible to lysis by 0.25% (w/v) sodium dodecyl sulphate and were permeable to certain enzyme substrates.
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PMID:Ultrastructural and chemical studies on wall-deficient forms, spheroplasts and membrane vesicles from Mycobacterium aurum. 703 68

Hairy-cell leukemia (HCL) is an unusual malignant hematologic disorder involving splenomegaly, pancytopenia, and circulating mononuclear cells with prominent cytoplasmic projections. As in most forms of leukemia, the risk of pulmonary infection by normal pathogens and opportunistic invaders alike is high. HCL may be associated with granulomatous infections of the lung, especially mycobacterioses. Of the authors' series of 33 patients, 9 had a fungal or mycobacterial infection, including 5 atypical mycobacterial species. Five of the 6 patients with mycobacterioses and 1 of the 3 with fungal pneumonia survived the infection with appropriate therapy. Granulomatous infections, particularly mycobacterioses, should be seriously considered in the differential diagnosis of pulmonary parenchymal disease in a patient with HCl.
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PMID:Pneumonia in hairy-cell leukemia. 720 21


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