Electrophoretic Analysis of Cell Proteins of T-Strain Mycoplasmas Isolated from Man

Razin, Shmuel; Valdesuso, J; Purcell, Robert H.; Chanock, Robert M.

doi:10.1128/jb.103.3.702-706.1970

Cited by 13 publications

(5 citation statements)

References 12 publications

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“…The propensity of ureaplasmas harvested after growth in vitro to be associated with noncellular materials from the growth medium has been previously observed (16,25,27). This has also been observed for some classical mycoplasmas and is known to influence the antigenic character (2,26,28) and the ability of the mycoplasmas to react in various diagnostic tests (4).…”

Section: Discussionmentioning

confidence: 70%

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Masover¹,

Razin²,

Hayflick³

1977

J Bacteriol

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Ureaplasma urealyticum cells were lysed by osmotic shock or by digitonin. The membrane fraction contained four to ten times as much protein as the cytoplasmic fraction. These values are in large excess of those reported for classical mycoplasmas, suggesting that the Ureaplasma membrane fraction was heavily contaminated with proteins derived from the growth medium. The U. urealyticum urease activity was localized in the cytoplasmic fraction, whereas the adenosine triphosphatase activity was localized in the membrane fraction. Significant urease activity could be detected also in nonviable cells. Urea, at concentrations above 0.25 M, was mycoplasmastatic to Acholeplasma laidlawii, Mycoplasma hominis, and U. urealyticum, so that the Ureaplasma urease did not afford preferential protection against urea toxicity. The intracellular localization of the urease would be expected to release ammonia from urea in the cytoplasm. The ammonia will take up protons to become ammonium ions. It can be hypothesized that the intracellular NH4+ plays a role in proton elimination or acid-base balance, which might be coupled to an energy producing ion gradient and/or transport mechanisms.

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Section: Discussionmentioning

confidence: 70%

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Masover¹,

Razin²,

Hayflick³

1977

J Bacteriol

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“…The lower ratio in the T mycoplasma could result from the presence of serum proteins contaminating the sedimented organisms. Since the yield of T mycoplasmas is so low, the small amounts of proteins from the medium that precipitate during growth and sediment together with the organisms on centrifugation may constitute a large percentage of the total protein in the pellet (9) and thus artificially reduce the values for labeled oleate incorporation or acetate utilization when expressed as radioactivity per milligram of protein.…”

Section: Resultsmentioning

confidence: 99%

Biosynthesis of saturated and unsaturated fatty acids by a T-strain mycoplasma (Ureaplasma)

Romano¹,

Rottem²,

Razin³

1976

J Bacteriol

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A human T mycoplasma (Ureaplasma urealyticum) incorporated radioactivity into its lipids from [1-'4C]acetate in the growth medium. Methanolysis of the lipids showed the label to be confined almost entirely to the methyl esters of the fatty acids. About 80% of the label was associated with the methyl esters of the saturated fatty acids, and the rest was found in the unsaturated methyl ester fraction. Gas-liquid chromatography of the saturated methyl esters showed the label to be present in the peaks of palmitate, myristate, and stearate, whereas in the unsaturated methyl ester fraction most of the radioactivity emerged in the peak of palmitoleate. The addition of either oleic or palmitic acid to the growth medium markedly decreased the organisms' incorporation of radioactivity from acetate. It is concluded that the T mycoplasma strain is capable of de novo synthesis of both saturated and unsaturated fatty acids, in this respect differing from all of the Mycoplasma and Acholeplasma strains investigated to date.

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“…-~All microorganisms except S. aureus (Smith parent) and its L-form were grown in Mycoplasma broth basal medium and provided with supplements according to their specific growth requirements. Proteins present in various media formulations have not been shown to interfere with cell protein electrophoretic patterns (12,14,17). Figure 1 shows the gel patterns of nine hULL.…”

Section: Resultsmentioning

confidence: 99%

Polyacrylamide Gel Identification of Bacterial L-Forms and Mycoplasma Species of Human Origin

Theodore

Tully

Cole

1971

Applied Microbiology

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Polyacrylamide gel electrophoretic patterns of acidified phenol extracts prepared from whole cells can be used for the identification of bacterial L-forms and Mycoplasma species of human origin. Ten human Mycoplasma serotypes and eight L-forms belonging to five different genera were studied. The gel patterns were sufficiently distinct and reproducible that it was possible not only to identify L-forms at the genus level (group with streptococci) and different Mycoplasma serotypes but also to differentiate between the two of them. The parentage of L-forms of Streptobacillus moniliformis Li, Listeria monocytogenes, Streptococcus MG, and Staphylococcus aureus Smith strain was established by relating their gel patterns directly to parent bacteria. It was found that an L-form designated S. moniliformis An (ATCC 14220) was actually an L-form of Proteus. In addition, it was shown electrophoretically that no relationship existed between the Streptococcus MG L-form and M. pneumoniae. The applicability of this method as a diagnostic and taxonomic tool for the differentiation of L-forms and mycoplasmas is discussed.

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Electrophoretic Analysis of Cell Proteins of T-Strain Mycoplasmas Isolated from Man

Abstract: Electrophoretic patterns of the cell proteins of 12 T-strain mycoplasmas isolated from man showed a remarkable similarity. This finding suggests that these strains are genetically closely related and supports their classification in a single species.

Cited by 13 publications

References 12 publications

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma)

Biosynthesis of saturated and unsaturated fatty acids by a T-strain mycoplasma (Ureaplasma)

Polyacrylamide Gel Identification of Bacterial L-Forms and Mycoplasma Species of Human Origin

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