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Two membrane fractions of intermediate density between inner and outer mitochondrial membranes were isolated by density gradient centrifugation from osmotically lysed mitochondria and mitoplasts of liver. These fractions were characterized by the presence of both monamine oxidase and cytochrome c oxidase activities and bound hexokinase. 1) The content of(More)
Human apolipoprotein C-I (apo C-I) in solution, in monomeric and oligomeric form, and in micellar complexes with dimyristoylphosphatidylcholine (DMPC), below and above the phase transition temperature of DMPC, was investigated with steady-state and time-resolved fluorescence methods. The environment of the Trp residue of apo C-I, in each physical state, was(More)
A simple purification of wheat germ agglutinin from commercial wheat germ is described. From defatted ground wheat germ, the lectin was extracted and then purified in a single step by filtration on an ion exchange chromatography column and adsorption on an insolubilized N-acetyl glucosamine derivative. The amount of lectin obtained from 1,000 g of wheat(More)
The tryptophyl fluorescence emission of yeast 3-phosphoglycerate kinase decreases from pH 3.9 to pH 7.2 following a normal titration curve with an apparent pK of 4.7. The fluorescence decays have been determined at both extreme pH by photocounting pulse fluorimetry and have been found to vary with the emission wavelength. A quantitative analysis of these(More)
The fluorescence quantum yield and the fluorescence decay of indole, 3-methylindole, 1-methylindole and N-acetyltryptophanamide have been measured in different water-dioxane mixtures. For the first three derivatives, the fluorescence decays were found independent of the emission wavelength and were analyzed as single exponential functions. In the case of(More)
Nanosecond-pulse fluorimetry of wheat germ agglutinin is analyzed as a function of both excitation and emission wavelengths. When excited at 280 nm, wheat germ agglutinin fluorescence exhibited three lifetimes: one corresponding to the tyrosine residues as a whole and two others corresponding to the tryptophyl emission. The tyrosine contribution to the(More)
The binding of clathrin and accessory coat proteins to small unilamellar vesicles and to liposomes of uncharged phospholipids has been followed by chromatography, 31P-NMR, ESR and fluorescence anisotropy. At pH 6.5 and at an ionic strength value (0.1 M Mes) close to that used during the purification of clathrin-coated vesicles, the proteins do not restore(More)