996 resultados para Day centre
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Performers from the Moscow Circus on float during May Day parade, Brisbane, Australia, 1968
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Members of the Inala Darra Peace Committee during Hiroshima Day 1964, Brisbane.
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Graceville and District Peace Committee members with banner during Hiroshima Day 1964, Brisbane, Australia.
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Holden utility carrying members of the Federated Ship Painters and Dockers Union during the Labour Day march in 1965, Brisbane, Australia. Anti conscription banners can be seen in the background, and the facade of the Pearl Assurance Building.
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Young Labor Association float during the Labour Day procession in Brisbane, Australia 1965. Placards call for voting rights for Aborigines, more education facilities and award wages.
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Boys with placard during the Labour Day procession in Brisbane, 1965.
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Notes for presentation
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Marchers including Bill Sutton during Labour Day procession in 1967 outside Exhibition Motors, Brisbane, Australia.
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Save our sons banner on float during May Day procession in Brisbane, Australia 1967. Other signs on truck include No conscription and Death lottery 1967.
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Woman with sash in sportscar during May Day procession, 1967, Queen Street, Brisbane, Australia. Onlookers stand outside a Queenslander house.
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Miss Equal Pay in sportscar during May Day procession, 1967, Queen Street, Brisbane, Australia.
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Members of the Union of Australian Women with banner during Hiroshima Day 1964, Brisbane, Australia. The Union of Australian Women is a national organisation that was formed in 1950. Its aim is to work for the status and wellbeing of women across the world. It has been involved in a wide variety of campaigns that concern women. The Union of Australian Women networks with other women's community and union groups on such issues.
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Electron paramagnetic resonance (EPR) spectra and X-ray absorption (EXAFS and XANES) data have been recorded for the manganese enzyme aminopeptidase P (AMPP, PepP protein) from Escherichia coli. The biological function of the protein, a tetramer of 50-kDa subunits, is the hydrolysis of N-terminal Xaa-Pro peptide bonds. Activity assays confirm that the enzyme is activated by treatment with Mn2+. The EPR spectrum of Mn2+-activated AMPP at liquid-He temperature is characteristic of an exchange-coupled dinuclear Mn(II) site, the Mn-Mn separation calculated from the zero-field splitting D of the quintet state being 3.5 (+/- 0.1) Angstrom. In the X-ray absorption spectrum of Mn2+-activated AMPP at the Mn K edge, the near-edge features are consistent with octahedrally coordinated Mn atoms in oxidation state +2. EXAFS data, limited to k less than or equal to 12 Angstrom(-1) by traces of Fe in the protein, are consistent with a single coordination shell occupied predominantly by O donor atoms at an average Mn-ligand distance of 2.15 Angstrom, but the possibility of a mixture of O and N donor atoms is not excluded. The Mn-Mn interaction at 3.5 Angstrom, is not detected in the EXAFS, probably due to destructive interference from light outer-shell atoms. The biological function, amino acid sequence and metal-ion dependence of E. coli AMPP are closely related to those of human prolidase, an enzyme that specifically cleaves Xaa-Pro dipeptides. Mutations that lead to human prolidase deficiency and clinical symptoms have been identified. Several known inhibitors of prolidase also inhibit AMPP. When these inhibitors are added to Mn2+-activated AMPP, the EPR spectrum and EXAFS remain unchanged. It can be inferred that the inhibitors either do not bind directly to the Mn centres, or substitute for existing Mn ligands without a significant change in donor atoms or coordination geometry. The conclusions from the spectroscopic measurements on AMPP have been verified by, and complement, a recent crystal structure analysis.