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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The polar lipids of the purple membrane were exchanged for different phosphatidylcholine species. The resulting complexes had the same protein to lipid-phosphorus ratio as the natural membrane, but only about 0.5-1.0 mole of original lipid was still present per mole of bacteriorhodopsin. In such complexes the bacteriorhodopsin photocycle is slowed down 10-20 times, but the strong protein-protein interaction is not abolished. Due to the slow rate of the photocycle we were able to measure in the light the ratio between net proton release and net accumulation of the last intermediate of the photocycle, the unprotonated M412. This ratio was not constant and equal to 1.0, as expected for a single deprotonation reaction, but varied with pH from 1.5 to 0.4. The variable ratio suggests that light-induced conformational changes occur in the nonchromophore part of the protein, which shift the pKa values of unidentified groups so as to cause binding or release of additional protons. A similar conclusion was drawn from experiments on the kinetics of proton transfer by bacteriorhodopsin in subbacterial particles of Halobacterium halobium and in reconstituted bacteriorhodopsin proteoliposomes. However, in this case light-induced association and dissociation of additional protons occurs simultaneously on different sides of the membrane.
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PMID:Bacteriorhodopsin: lipid environment and conformational changes. 2 25

Neomycin phosphate was obtained as a result of neomycin phosphorylation with aminoglycoside-phosphotransferase from Act. fradiae. It was isolated from the reaction mixture and purified. Successive ion exchange chromatography on columns with Amberlite IRC-50 (NH+4 form), Dowex 1 X 10 (OH- form) and Amberlite CG-50 (NH+4 form) was used for purification of the inactivation product. The findings of the elementary analysis of neomycin phosphate showed the presence of 1 mole of phosphorus per 1 mole of the antibiotic. From the results of the chemical analysis, IR- and NMR-spectrometry neomycin phosphate and neamine phosphate obtained from it by methanolysis were identified as neomycin-3'-phosphate and neamine-3'-phosphate, respectively. The data indicate that the enzyme isolated from Act. fradiae is aminoglycoside-3'-phosphotransferase.
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PMID:[Aminoglycoside-3'-phosphotransferase from Actinomyces fradiae. The identification of its inactivation product]. 3 33

Changes in the structural components of the Streptococcus pyogenes membrane between exponential and early stationary phases of growth are reported. The overall protein composition ranged from 70 to 73% of the dry weight of the membranes, irrespective of the phase of growth from which they were isolated. Amino acid analyses of membranes isolated from streptococci in either the exponential or stationary phase of growth demonstrated that two amino acids, cysteine and tryptophan, were absent. Further analysis of the membrane proteins by sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis demonstrated that there were proteins unique to a particular phase of growth as well as differences in the amount of specific proteins from the various growth phases. In addition, membranes isolated from exponential-phase cultures contained a higher percentage of peripheral protein than did stationary-phase membranes. There also appeared to be an increase in the amount of outer surface proteins during this growth phase. The phosphorus content of the membranes increased during the stationary phase of growth, whereas the sugar composition remained constant. The only sugar found under various conditions of growth in any of the strains was glucose. Total fatty acid content and the mole percent composition of various fatty acids did not change in the different phases of growth. However, the mole percent composition of fatty acids in the membranes of various group A streptococci did differ between strains. Therefore, these results provide evidence that the composition of membranes of S. pyogenes does not remain constant throughout the growth phases of the culture.
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PMID:Chemical analysis of changes in membrane composition during growth of Streptococcus pyogenes. 16 Aug 90

A white woman with unilateral nevus of Ota presented with visual loss and an intraocular mass resembling a choroidal melanoma. Indirect ophthalmoscopy, fluorescein angiography, ultrasonography, and radioactive phosphorus uptake corroborated the clinical impression and surgery was advised. Following enucleation, the specimen was examined with light microscopy, which revealed a mixed cell type malignant melanoma of the choroid. Electron microscopy disclosed the presence of premelanosomes in the episclera, indicating that the episcleral pigmentation is a result of melanocytic evolution. This paper represents the tenth report in the literature of choroidal melanoma occurring in a patient with nevus of Ota, and the first electron-microscopic study of an eye with this association of lesions.
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PMID:Malignant melanoma of choroid in a case of nevus of Ota. 43 36

An elevated pigmented mass of the choroid remained stable for 6 1/2 years and then was documented photographically to have increased in size. The tumor stained on fluorescein angiography, produced a visual field defect, and differentially took up radioactive phosphorus. The eye was enucleated and on histologic examination contained a nevus of the choroid. This case shows that enlargement of a choroidal nevus may occur during adulthood, and suggests that despite newer and more sophisticated diagnostic techniques, large nevi and small melanomas of the choroid may be clinically indistinguishable.
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PMID:Enlargement of a histologically documented choroidal nevus. 44 11

A chorioretinal granuloma that contained acid-fast bacilli and a choriodal nevus that consisted of benign nevus cells yielded false-positive radioactive phosphorus tests. The beta emission exceeded that of the control areas by more than 100% in each case. The granuloma had infiltrated the sclera, permitting inflammatory tissue to be in closer proximity to the counting probe than was the normal choroid. The reason for the increased metabolic activity of the nevus cells remains unexplained.
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PMID:False-positive results with the radioactive phosphorus test. 58 12

Doxyribonucleates (DNMe) and deoxyribonucleic acid (DNA) were prepared by the ion-exchange method from Na+-salt from chicken erythrocyte DNA (DNS). (Here Me+ means Rb+, CS+, Na+, or NH4+). It was found that in aqueous solutions of DNMe in which the concentration of nucleic phosphorus was 8-10(5) mole/1 and the supporting electrolyte contained as an impurity only, the secondary structure of DNA was partly restored. This was confirmed by low values of the atomic extinction coefficient (epsilon260(p) = 6800 1/mole-cm and by high values of the hyperchromicity coefficients (1-28). The melting temperatures, as well as the width of the melting transition calculated from the melting curves, did not depend on the nature of Me+. Abnormally high melting temperatures for aqueous solutions of DNMe were noted. It was shown that the DNS - DNA transition was accompanied by spectrum changes that are typical of the denaturation process.
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PMID:[Effect of the nature of a monovalent counterion on the secondary structure of DNA is aqueous solutions]. 84 8

A new method for quantitation of ovalbumin by thin layer isoelectric focusing in polyacrylamide gel is described. This technique separates ovalbumin from avian-magnum homogenates or egg white and allows the quantitative determination of each ovalbumin fraction. Considering the very small amount (7 mul) of sample needed for an analysis, the sensitivity and the reproducibility of the proposed method are good. The application of this technique to quail egg white ovalbumin analysis leads to the characterization of four fractions A3, A2, A1 and A0 containing, respectively, 0, 1, 2 and 3 atoms of phosphorus per mole and with isoelectric points that range from 4.95 (A3) to 4.65 (A0).
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PMID:[Quantitative analysis of ovalbumin by thin-layer isoelectric focusing (author's transl)]. 99 80

In 21 patients with a variety of skin tumors (squamous cell carcinomas, malignant melanomas, basal cell epitheliomas and mycosis fungoides) or pre-cancerous lesions (Bowen's disease, actinic keratosis, junctional nevus cell nevus) the radioactive phosphorus uptake test demonstrates a significantly increased concentration of P32 in those tumors. There were no false negative tests. The possibility of differentiation of malignant melanoma from benign nevus cell nevus and the early recognition of cutaneous metastases is described. Furthermore recurrence of previously irradiated or excised basal cell epitheliomas can be detected without a biopsy. No hematological side-effects were observed.
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PMID:[The radiophosphorus (32P)-test in precanceroses and malignant tumors of the skin]. 127 Feb 58

The influence of cytochrome c binding to cardiolipin bilayers on the motional characteristics of each component has been analyzed by magic-angle spinning (MAS) NMR. Observations were made by NMR of natural abundance 31P, 13C, and 1H nuclei in the lipid as well as sites enriched with 13C in the protein. Analysis of methyl carbons enriched in ([epsilon-13CH3]methionine)cytochrome c at residues 65 and 80 reveal quite different behavior for these sites when the protein was bound at a 1:15 molar ratio with hydrated cardiolipin. Cross-polarization (CP) shows a single broad resonance downfield in the methyl region which corresponds to the spectral characteristics of methionine 65 in the solution protein when subjected to moderate thermal perturbations. These observations suggest that although methionine 65 remains motionally restricted when the protein binds to the lipid bilayers, this residue becomes less shielded and exposed to more chemically distinct environments than in the native state of the protein. In contrast to its behavior in native oxidized protein, the methionine 80 methyl could be detected following direct pi/2 pulse excitation, and this residue is assumed to be released from the axial ligand site on the heme iron to become more exposed and highly mobile in the protein-lipid complex. An analysis of the CP response for natural abundance 13C nuclei in the lipid reveals a general increase in motions with slower rates (tens of kilohertz) on binding with cytochrome c, except for sites within the region of fatty acyl chain unsaturation which appear to be selectively mobilized in the complex with protein. It is concluded that, aside from effects on the unsaturated segments, the bound protein induces new modes of slow motions in the lipid assemblies rather than restricting the overall reorientation freedom of the lipid. The strong paramagnetic effects observed previously on the relaxation of phosphorus in protein-bound lipid [Spooner, P.J.R., & Watts, A. (1991) Biochemistry 30, 3880-3885] were not extended to any carbon and proton sites observable by MAS NMR in the lipid, and this infers a specific interaction of lipid phosphate groups with the heme. However, when protein was bound to cardiolipin mixed at a 1:4 mole ratio with dioleoylphosphatidylcholine in bilayers, no direct interaction with the heme was apparent from the phosphorus NMR relaxation behavior in this component, resolved by MAS. Instead, the spectral anisotropy of cardiolipin phosphorus was determined to be reduced, indicating that, on binding with cytochrome c, the headgroup organization was perturbed in this component.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study. 132 34


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