A totally nonempirical relativistic cluster calculation of transition-metal L 2,3 -edge x-ray-absorption nearedge structure including configuration interaction has been performed. A remarkable predictive power of this calculation has been demonstrated for three contrasting materials with different d-electron numbers and different coordination numbers ͑SrTiO 3 , NiO, and CaF 2 ͒ by excellent reproduction of both the absolute peak energies and their relative intensities without any empirical parameters.

Human alpha 1-proteinase inhibitor was purified according to a modification of the method of Kurecki et al. (Anal. Biochem. 99, 415 (1979) ), with Affi-Gel Blue treatment before Zn-affinity column chromatography. The inhibitor was inactivated in the presence of Pseudomonas aeruginosa elastase (1/2,000 molar ratio) for 2 h at pH 7.5 and 25 degrees C. The inactivated inhibitor was purified by column chromatography on Sephadex G-75 and DE-52. Little or no difference was observed between the native and inactive inhibitors in immunological response, amino acid composition or far-ultraviolet CD spectrum. On the other hand, a considerable difference was observed in the near-ultraviolet CD spectrum. Two amino-terminal sequences were found in the inactive inhibitor in almost the same ratio; one was the same as that of the intact inhibitor and the other was Met-Ser-Ile-Pro-. The two components were separated by high-performance liquid chromatography using 0.1% trifluoroacetic acid containing 30-70% CH3CN (gradient) as the eluent. Amino acid analysis and N- and C-terminal amino acid sequence analyses indicated that one fraction corresponded to the sequence of 1-357 of the alpha 1-proteinase inhibitor and the other to 358-394. We concluded that P. aeruginosa elastase can inactivate human alpha 1-proteinase inhibitor by splitting the peptide bond of Pro357-Met358, leading to local change near the active site but little change in the structure as a whole. The split carboxy-terminal fragment binds tightly to the rest of the inhibitor.

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FH, FW, and CSA of the IVF, except for L5/S1, decreased significantly during axial loading. Changes in posterior DH correlated well with the changes in foraminal dimensions.

Endocytic pathwaysa re practical routes for the intracellular delivery of biomacromolecules.A long with this, effective strategies for endosomal cargo release into the cytosol are desired to achieve successful delivery.F ocusing on compositional differences between the cell and endosomal membranes and the pH decrease within endosomes,w e designed the lipid-sensitive and pH-responsive endosome-lytic peptide HAad. This peptide contains aminoadipic acid (Aad) residues,w hichs erve as as afety catch for preferential permeabilization of endosomal membranes over cell membranes,a nd His-to-Ala substitutions enhance the endosomolytic activity.T he ability of HAad to destabilizee ndosomal membranes was supported by model studies using large unilamellar vesicles (LUVs) and by increased intracellular delivery of biomacromolecules (including antibodies) into live cells.C erebral ventricle injection of Cre recombinase with HAad led to Cre/loxP recombination in am ouse model, thus demonstrating potential applicability of HAad in vivo.