The Escherichia coli ATP-dependent protease Lon degrades ribosomal S2 protein in the presence of inorganic polyphosphate (polyP). In this study, the process of the degradation was investigated in detail. During the degradation, 68 peptides with various sizes (4-29 residues) were produced in a processive fashion. Cleavage occurred at 45 sites, whose P 1 and P 3 positions were dominantly occupied by hydrophobic residues. These cleavage sites were located preferentially at the regions with rigid secondary structures and the P 1 residues of the major cleavage sites appeared to be concealed from the surface of the substrate molecule. Furthermore, polyP changed not only the substrate preference but also the oligomeric structure of the enzyme.

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Twenty-five vision-impaired diabetics received an evaluation of sensibility. Each subject had received 2 years of instruction in braille reading at the Konan Rehabilitation Center prior to the sensibility testing. Sensibility evaluation consisted of cutaneous pressure threshold measurements with the Semmes-Weinstein monofilament and evaluation of moving and static two-point discrimination with Disk-Criminator. The ability to read braille was graded by the braille-teaching instructors as good, fair, and unable. The results of the evaluation of sensibility demonstrated that the value of the cutaneous pressure threshold did not correlate with the ability to read braille. Moving and static two-point discrimination were found to correlate highly (P less than .001) with the ability to read braille at a level of fair or good. No patient in this study with a moving two-point discrimination value of 4 or more or a static two-point discrimination value of 5 or more was able to read braille even at the fair level of ability.

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