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Query: UMLS:C0026936 (Mycoplasma)
 14,761 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The properties of the membrane-bound reduced nicotinamide adenine dinucleotide (NADH) oxidase of Acholeplasma laidlawii were compared with those of the corresponding cytoplasmic activity of Mycoplasma mycoides subsp. capri. The striking differences in pH optima, susceptibility to inhibitors and detergents, and heat inactivation between the NADH oxidase activity, with oxygen as an electron acceptor, and the NADH oxidoreductase activity, with dichlorophenol indophenol (DCPIP) as an alternate electron acceptor, support the presence of more than one catalytic protein in both the membrane-bound and soluble enzyme systems. The detection of more than one band positive for the NADH-nitroblue tetrazolium oxidoreductase reaction on electrophoresis of either the membranes of A. laidlawii or the cytoplasm of M mycoides subsp. capri also points in the same direction. The membrane-bound enzyme system differed, however, form the soluble one because it had a lower ratio of oxidase activity to oxidoreductase activity, and because it was less susceptible to heat inactivation and more readily incorporated incorporated into reaggregated membranes. In addition, the specific activity of the membrane-bound enzyme system increased as the culture aged, whereas that of the soluble system decreased as the culture aged. It is suggested that the different location in the cell could be responsible for some of the differences between the membrane-bound NADH oxidase activity of A. laidlawii and that found in the cytoplasm of M. mycoides subsp. capri.
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PMID:Reduced nicotinamide adenine dinucleotide oxidase activity in membranes and cytoplasm of Acholeplasma laidlawii and Mycoplasma mycoides subsp. capri. 1 Dec 8

Mycoplasma synoviae was tested for its ability to grow and induce cytopathogenic changes in chicken embryo cell cultures. M. synoviae grew to high titers by day 5 in the presence of chick cells, but showed no growth in the tissue culture medium alone even though it was enriched with nicotinamide adenine dinucleotide and swine serum. Infected chick cell cultures showed a progressive cytoplasmic degeneration on successive days of examination. Early changes involved cytoplasmic granularity and mild vacuolation. On the last day of examination the cytoplasm of most cells was completely degenerated and some showed nuclear degeneration. M. synoviae was shown to be cytophilic for the chick cell membranes where the mycoplasmas reproduced and formed microcolonies which, on successive days, increased in size. The attachment site on the chick cell membrane was shown to be neuraminidase sensitive.
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PMID:Growth and cytopathology of Mycoplasma synoviae in chicken embryo cell cultures. 16 27

The cultivation of Mycoplasma synoviae (MS) on growth medium requires supplementation with B-nicotinamide adenine dinucleotide (NAD), an expensive and relatively unstable compound. Strains of MS were adapted (selected) to grow in a medium supplemented instead with nicotinamide, a stable and inexpensive substance that can be heat-sterilized in the medium without impairing its growth-promoting properties. MS plate agglutinating antigens grown in nicotinamide-enriched media were comparable in yield and serological reaction to antigens grown with NAD supplementation.
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PMID:Growth of Mycoplasma synoviae in a medium supplemented with nicotinamide instead of B-nicotinamide adenine dinucleotide. 16 2

Spiroplasma citri was cultured in three different media that supplied cholesterol and fatty acids from: (i) horse serum, (ii) pleuropneumonia-like organism (PPLO) serum fraction, or (iii) bovine serum albumin-fatty acid-cholesterol. The ability of PPLO serum fraction to support growth varied by lot number. Neither PPLO serum fraction nor the bovine serum albumin medium supported growth as well as the horse serum medium. Analysis of cholesterol, lipid phosphorus, and membrane protein showed the horse serum- and PPLO-grown cells to be indistinguishable, but the bovine serum albumin-grown cells were deficient in lipid phosphorus. The three cultures did not show markedly different fatty acid compositions, but, in all cases, the cultures preferentially incorporated palmitic acid and discriminated against linoleic acid. Cultures grown for different times from logarithmic growth through a degenerative phase showed relatively constant ratios of cholesterol/protein and lipid phosphorus/protein. Fatty acid composition was also relatively constant at the different stages. Adenosine triphosphatase and p-nitrophenyl phosphatase were mainly associated with the membrane, whereas reduced nicotinamide adenine dinucleotide oxidase was either readily removed or not associated with the membrane. The reduced nicotinamide adenine dinucleotide oxidase was inactivated at temperatures above 35 degrees C.
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PMID:Composition and enzyme activities of Spiroplasma citri membranes. 19 32

Mycoplasma laidlawii possesses a single glutamate dehydrogenase (GDH) with dual coenzyme specificity [specificity for nicotinamide adenine dinucleotide (H) and nicotinamide adenine dinucleotide phosphate (H)]. A purification procedure is reported which results in an enzyme preparation with a specific activity of 79.5 units/mg and which displays only one significant protein band after gel electrophoresis. This one band was determined, by activity staining, to have all of the GDH nucleotide specificities. The molecular weight of the enzyme is 250,000 +/- 10%, and it has a subunit size of about 48,000. The enzyme exhibits measurable activity with aspartate and pyruvate but is inactive with eight other possible substrates. Purine nucleotides do not affect the activity. The K(m) for reduced nicotinamide adenine dinucleotide was 1.8 x 10(-4)m. The optimal substrate concentrations and pH optimum for each of the respective GDH activities are also reported.
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PMID:Glutamate dehydrogenase from Mycoplasma laidlawii. 411 54

Eight fermentative mycoplasmas differing in genome size, deoxyribonucleic acid (DNA) base composition, or sterol dependence were examined for lactic dehydrogenase composition by spectrophotometric assay and polyacrylamide gel electrophoresis. Three completely different patterns of lactic dehydrogenase composition were found. (i) A nicotinamide adenine dinucleotide (NAD)-dependent l(+)-lactic dehydrogenase was found in Mycoplasma pneumoniae, M. gallisepticum, M. mycoides var. mycoides, mycoplasma UM 30847, M. neurolyticum, and Acholeplasma axanthum. Electrophoresis of cell-free extracts of each of these mycoplasmas produced, with the exception of M. mycoides var. mycoides and UM 30847, single, different enzyme bands. M. mycoides var. mycoides and UM 30847 were similar and formed multiple bands of enzyme activity. We were unable to establish whether these multiple bands were due to lactic dehydrogenase isoenzymes or artifacts. (ii) An NAD-dependent d(-)-lactic dehydrogenase which could not be reversed to oxidize lactate was found in M. fermentans. (iii) A. laidlawii A possessed an NAD-independent d(-)-lactic dehydrogenase capable of reducing dichlorophenol-indophenol, and an NAD-dependent l(+)-lactic dehydrogenase which is specifically activated by fructose-1,6-diphosphate. Heretofore, this enzyme regulatory mechanism was known to occur only among the Lactobacillaceae. No yeast-type lactic dehydrogenase activity was found in any of the mycoplasmas examined. The stereoisomer of lactic acid accumulated during growth correlated perfectly with the type of NAD-dependent lactic dehydrogenase found in each mycoplasma. The types of lactic dehydrogenase activity found in these mycoplasmas were not related to genome size, DNA base composition, or sterol dependence.
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PMID:Occurrence and properties of lactic dehydrogenases of fermentative mycoplasmas. 411 65

Cell-free extracts of Mycoplasma pneumoniae showed two distinct reduced nicotinamide adenine dinucleotide (NADH(2)) oxidase activities in the supernatant fraction. By ammonium sulfate fractionation and polyacrylamide gel electrophoresis, one activity not requiring flavine co-factors was precipitated by 50 to 70% ammonium sulfate concentration and identified with a slower-moving band on acrylamide gel electrophoresis; a second NADH(2) oxidase activity was flavine mononucleotide (FMN) dependent and associated with a more rapidly moving band; it could only be partially precipitated by ammonium sulfate concentrations ranging from 50 to 100%. Studies with alternate electron acceptors indicated the presence of a menadione, a 2,6-dichlorophenol indophenol and a very weak ferricyanide oxido-reductase activity, but no cytochrome c oxido-reductase, in the cell-free preparations. The NADH(2) oxidase activities of all fractions were relatively cyanide insensitive and were only minimally inhibited by flavoprotein and other respiratory chain inhibitors. H(2)O(2) formation was negligible unless FMN, but not flavine adenine dinucleotide (FAD), was added to the crude NADH(2) oxidase system; upon fractionation and electrophoresis, the H(2)O(2) formation was associated with the FMN-dependent, more rapidly moving NADH(2) oxidase band. This FMN-dependent NADH(2) oxidase-H(2)O(2) generating system may be a mechanism for the H(2)O(2) formation observed during glucose oxidation in the intact organism.
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PMID:Reduced nicotinamide adenine dinucleotide oxidase activity and H2O2 formation of Mycoplasma pneumoniae. 414 46

A highly significant correlation coefficient (r = 0.97, n = 18) was found between the concentration of lactate dehydrogenase measurable after the organisms had been disrupted and the concentration of colony-forming units during the logarithmic phase of growth of a broth culture of the T(1) strain of Mycoplasma mycoides var. mycoides. A concentration of 4.60 x 10(-7) milliunits of lactate dehydrogenase for each colony-forming unit was established. This relationship was used to convert the concentration of lactate dehydrogenase in the culture into an estimate of the concentration of viable mycoplasma. The lactate dehydrogenase was estimated by following the oxidation of reduced nicotinamide adenine dinucleotide, in the presence of pyruvate substrate, at 366 nm in a spectrophotometer. The nicotinamide adenine dinucleotide oxidase system probably contributed a small amount of enzyme activity to the test when lactate dehydrogenase was measured in this way. The method has been described and evaluated for the estimation of titers from 10(7) to 5 x 10(9) colony-forming units per ml.
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PMID:Estimation of the growth of the T 1 strain of Mycoplasma mycoides in tryptose broth by the measurement of lactate dehydrogenase. I. Method. 433 38

Various physiological important activities of Mycoplasma gallisepticum were inhibited by the copper(I) complex of 2,9-dimethyl-1,10-phenanthroline [Cu(DMP)2NO3]. The energy-yielding metabolism was inhibited because the conversion of pyruvate into lactate was found to be blocked by Cu(DMP)2NO3, indicating a selective inhibition of lactate dehydrogenase. Also, the production rate of acetate and the rate of oxygen uptake by whole cells of M. gallisepticum appeared to be strongly decreased. Experiments with crude cell extracts showed an inhibition of reduced nicotinamide adenine dinucleotide (NADH) oxidase by Cu(DMP)2NO3 and an even stronger inhibition of NADH oxidase and lactate dehydrogenase by CuSO4. No preferential inhibition of adenosine 5'-triphosphatase and pyruvate kinase was found. Investigations on the influence of Cu(DMP)2NO3 on deoxyribonucleic acid, ribonucleic acid, and protein synthesis with growing cells of M. gallisepticum showed a selective inhibition of the incorporation of [14C]thymidine into deoxyribonucleic acid. Cu(DMP)2NO3 induced a decrease in the total amount of accessible sulfhydryl groups of whole cells of M. gallisepticum, indicating that the observed diverse toxicity of Cu(DMP)2NO3 may be associated with the interaction of copper ions with protein sulfhydryl groups.
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PMID:Mode of action of the copper(I) complex of 2,9-dimethyl-1,10-phenanthroline on Mycoplasma gallisepticum. 617 82

The type strain WVU 1853 and field strains SG, N26 and A642 of Mycoplasma synoviae were examined for their requirement for nicotinamide-adenine dinucleotide (NAD) for in vitro growth. All the strains grew and could be repeatedly passaged in Frey broth medium supplemented with filter-sterilised NAD. In modified Frey broth medium from which NAD was omitted and broth medium for which the supplements including yeast extract and NAD were autoclaved, only strains N26 and A642 could be grown and passaged. The growth curves of strain N26 determined in broth media with and without NAD were similar. These results indicated that there are differences in NAD-requirement for in vitro growth among strains of M synoviae.
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PMID:Diversity in nicotinamide-adenine dinucleotide requirement for the growth of different strains of Mycoplasma synoviae. 652 30


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