Setting physical standards for mental hospitals: to whom should the courts listen?
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Commitment of Persons with Psychiatric Disorders↗
Biomedical subjects
J O'Reilly
Publications and source records attributed to J O'Reilly.
Involvement of adenosine 3':5'-cyclic monophosphate in the germination of blastospores of Candida albicans.
The germination of blastospores of Candida albicans is accompanied by a rise in the intracellular concentration of adenosine 3':5'-cyclic monophosphate (cyclic AMP). Germination was induced either by peptides isolated from seminal plasma or by an amino acid mixture, and both germination and the rise in cyclic AMP required a temperature of 37 degrees C. The rise occurred during the first hour of incubation, but full germination required a temperature of 37 degrees C for 4 h. Germination and the rise in cyclic AMP, in the presence of suboptimal concentrations of inducers, were stimulated by theophylline. Pre-incubation of cells with dithiothreitol in the absence of inducers inhibited subsequent germination but not the rise in cyclic AMP. Germination and the rise in cyclic AMP were inhibited if dithiothreitol or N-succinimidyl-3-(4-hydroxyphenyl)propionate was present during the induction period.
Bucladesine↗
Purification and properties of peptides which induce germination of blastospores of Candida albicans.
A glycopeptide and a peptide have been isolated from bovine seminal plasma which together will induce germination of Candida albicans blastospores at 37 degrees C and in the presence of glucose and Mn2+. ¿They have molecular weights of 2000 to 3000. Both peptides contain appreciable amounts of aspartic and glutamic acids, only the glycopeptide contains threonine, lysine, histidine and arginine, while only the peptide contains proline. Acid hydrolysates are fully active in inducing germination and a mixture of aspartic acid, lysine, histidine, threonine, proline and beta-alanine can replace them. Mn2+ is not then required. Amino acid mixtures are required to be present throughout the whole period in the incubation medium for full germination to take place, but the peptides can be removed after 1 h incubation and if the cells are resuspended in a buffered glucose medium full germination occurs after a further 3 h incubation.
Amino Acids↗
Changes in the cell surface of the dimorphic forms of Candida albicans by treatment with hydrolytic enzymes.
The release of acid phosphatase and polysaccharide-peptide complexes by hydrolytic enzymes from the surface of the blastospore and mycelial forms of Candida albicans has been examined in cells from 4 h and 18 h cultures and the results correlated with the appearance of the treated cells in the electron microscope. Treatment with dithiothreitol was necessary for the degradative action of the enzymes to occur. Material released by all the treatments used had a similar qualitative composition, but the proportions of mannan, glucan, peptide and acid phosphatase varied with different treatments and with the type of cell examined. I,3-beta-Glucanase was required for major changes in the cell wall to be effected, but a significant amount of material was released with a chitinase preparation containing some protease activity. Protoplasts were obtained from all types of cell using Cytophaga lytic enzyme L1 which had I,3-beta-glucanase and protease activity, but the purified I,3-beta-glucanase and protease prepared from Streptomyces violaceus cultures required the presence of a chitinase before protoplasts were released. The bonding association between the major components which comprise the cell wall, and the spatial distribution of these macromolecules, varies appreciably between the two dimorphic forms and with the age of the culture.
Acid Phosphatase↗
Induction of the mycelial form of Candida albicans by hydrolysates of peptides from seminal plasma.
Previous work led to the separation from seminal plasma of a peptide fraction which promoted a high rate of germination of blastospores of Candida albicans. It has now been shown that an acid hydrolysate of this material is also highly active. A minimal amino-acid mixture consisting of aspartic acid, lysine, histidine, threonine, proline and beta-alanine gave 90% germination in 4 h with 17 out of 28 strains examined. Glucose and inorganic phosphate were also required. Phosphate was not required for the activity of the original peptide fraction.
Amino Acids↗
Antibacterial sesquiterpene aryl esters from Armillaria mellea.
Investigation of the mycelial extract of Armillaria mellea led to the isolation of the known melleolide (2a) and two new sesquiterpene aryl eters, 4-O-methylmelleolide (2b) and judeol (1c). Their structures were deduced from spectral data and that of (2b) confirmed by X-ray analysis. The new esters (1c) and (2b) showed strong antibacterial activity against gram-positive bacteria.
Agaricales↗
Expression, purification and secondary structure analysis of Saccharomyces cerevisiae vacuolar membrane H+-ATPase subunit F (Vma7p).
The vacuolar H+-ATPase is an acid pump found in virtually all eukaryotic cells. It shares a common macromolecular organization with the F1F0-ATPase, and some V-ATPase subunits are structural and functional homologues of F-ATPase components. However, the vacuolar complex contains several subunits which do not resemble F-ATPase subunits at the sequence level, and which currently have no specific function assigned. One example is subunit F, the Vma7p polypeptide of Saccharomyces cerevisiae. A recombinant form of Vma7p was expressed in Escherichia coli and purified to homogeneity. Mass spectroscopy confirmed a mass of 13460 Da for Vma7p, and dynamic light scattering showed that the polypeptide was globular and monodisperse even at high concentrations. Analysis of secondary structure by circular dichroism and FTIR showed that Vma7p comprises 30% alpha-helix and 32-42% beta-sheet. The protein fold recognition programme 'Threader 2' produced highly significant matches between Vma7p and five alpha-beta sandwich folds. Relative proportions of secondary structure elements within these folds were broadly consistent with the spectroscopic data. Although Vma7p does not share sequence similarity with the F-ATPase epsilon subunit, the analysis suggests that the polypeptides not only have similar masses and assemble into homologous core complexes, but also share similar secondary structures. It is possible that the two polypeptides are homologous and perform similar functions within their respective ATPases. The production of high yields of homogeneous, folded, monodisperse protein will facilitate high resolution crystallography and NMR spectroscopy studies.
Circular Dichroism↗