977 resultados para Anastasius I, Emperor of the East, ca. 430-518.
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[In 8 separately paged parts, each vol. containing 2 pts.]
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Mode of access: Internet.
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Mode of access: Internet.
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Mode of access: Internet.
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Each volume has also special t.p.
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Mode of access: Internet.
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Includes index.
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Mode of access: Internet.
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Added title page: The autobiography and recollections of Laura, duchess of Abrantès (widow of General Junot) : with reminiscences of her life in Corsica, Paris, and in Spain and Portugal.
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Bathymetric data from a Hydrosweep multibeam sonar survey of a 720 km long tectonic corridor on the east flank of the southern EPR at 14 degrees 14'S covered about 25,000 km(2) of zero-age to 8.5 m.y. old crust (magnetic anomaly 4A). In this corridor we document a strong correlation of robust along flowline changes in abyssal hill morphology and seamount size distribution with spreading rate changes deduced from our magnetic data. Indeed, we find that both rms height of abyssal hills and abundance and height of seamounts increase significantly as spreading rate changes from similar to 75 mm/yr to over 85 mm/yr (half rate). Moreover, we identified 46 seamounts taller than 100 m. Previous studies on the southern EPR reported a larger density of seamounts, organized primarily in chains. Our investigation, however, revealed seamounts not associated with major chains, leading us to the conclusion that different forms of off-axis volcanism occur along the spreading center.
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Microsomes (105,000xg sediment) prepared from induced cells of A.ochraceus was found to hydroxylate progesterone to 11-Alpha-hydroxyprogesterone (11a-OHP) in high yields (85-�90% in 30 min.) in the presence of NADPH and O2. The pH optimum for the hydroxylase was found to be 7.7. However, for the isolation of active microsomes grinding of the mycelium should be carried out at pH 8.3. Metyrapone, carbon monoxide, SKF-525A, p-CMB and N-methyl maleimide inhibited the hydroxylase activity indicating the involvement of cytochrome P-450 system. The inhibition of the hydroxylase by cytochrome Image and the presence of high levels of NADPH-cytochrome Image reductase in induced microsomes suggest that the reductase could be one of the components in the hydroxylase system.
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Microsomes (105,000xg sediment) prepared from induced cells of Image was found to hydroxylate progesterone to 11a-hydroxyprogesterone (11a-OHP) in high yields (85-90% in 30 min.) in the presence of NADPH and O2. The pH optimum for the hydroxylase was found to be 7.7. However, for the isolation of active microsomes grinding of the mycelium should be carried out at pH 8.3. Metyrapone, carbon monoxide, SKF-525A, p-CMB and N-methyl maleimide inhibited the hydroxylase activity indicating the involvement of cytochrome P-450 system. The inhibition of the hydroxylase by cytochrome Image and the presence of high levels of NADPH-cytochrome Image reductase in induced microsomes suggest that the reductase could be one of the components in the hydroxylase system.
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The novel multidomain organization in the multimeric Escherichia coli AHAS I (ilvBN) enzyme has been dissected to generate polypeptide fragments. These fragments when cloned, expressed and purified reassemble in the presence of cofactors to yield a catalytically competent enzyme. Structural characterization of AHAS has been impeded due to the fact that the holoenzyme is prone to dissociation leading to heterogeneity in samples. Our approach has enabled the structural characterization using high-resolution nuclear magnetic resonance methods. Near complete sequence specific NMR assignments for backbone H-N, N-15, C-13 alpha and C-13(beta) atoms of the FAD binding domain of ilvB have been obtained on samples isotopically enriched in H-2, C-13 and N-15. The secondary structure determined on the basis of observed C-13(alpha) secondary chemical shifts and sequential NOEs indicates that the secondary structure of the FAD binding domain of E. coli AHAS large Subunit (ilvB) is similar to the structure of this domain in the catalytic subunit of yeast AHAS. Protein-protein interactions involving the regulatory subunit (ilvN) and the domains of the catalytic subunit (ilvB) were studied using circular dichroic and isotope edited solution nuclear magnetic resonance spectroscopic methods. Observed changes in circular dichroic spectra indicate that the regulatory subunit (ilvN) interacts with ilvB alpha and ilvB beta domains of the catalytic subunit and not with the ilvB gamma domain. NMR chemical shift mapping methods show that ilvN binds close to the FAD binding site in ilvB beta and proximal to the intrasubunit ilvB alpha/ilvB beta domain interface. The implication of this interaction on the role of the regulatory subunit oil the activity of the holoenzyme is discussed. NMR studies of the regulatory domains show that these domains are structured in solution. Preliminary evidence for the interaction of ilvN with the metabolic end product of the pathway, viz., valine is also presented.