9 research outputs found

    Semi-Automatic Calibration Method for a Bed-Monitoring System Using Infrared Image Depth Sensors

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    With the aging of society, the number of fall accidents has increased in hospitals and care facilities, and some accidents have happened around beds. To help prevent accidents, mats and clip sensors have been used in these facilities but they can be invasive, and their purpose may be misinterpreted. In recent years, research has been conducted using an infrared-image depth sensor as a bed-monitoring system for detecting a patient getting up, exiting the bed, and/or falling; however, some manual calibration was required initially to set up the sensor in each instance. We propose a bed-monitoring system that retains the infrared-image depth sensors but uses semi-automatic rather than manual calibration in each situation where it is applied. Our automated methods robustly calculate the bed region, surrounding floor, sensor location, and attitude, and can recognize the spatial position of the patient even when the sensor is attached but unconstrained. Also, we propose a means to reconfigure the spatial position considering occlusion by parts of the bed and also accounting for the gravity center of the patient’s body. Experimental results of multi-view calibration and motion simulation showed that our methods were effective for recognition of the spatial position of the patient

    Precise Indoor Localization Method Using Dual-Facing Cameras on a Smart Device via Visible Light Communication

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    Proteinase Inhibitor from Ginkgo Seeds Is a Member of the Plant Nonspecific Lipid Transfer Protein Gene Family1

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    A 9-kD proteinase inhibitor was isolated from the seeds of ginkgo (Ginkgo biloba) and purified to homogeneity. This protein was revealed to partial-noncompetitively inhibit the aspartic acid proteinase pepsin and the cysteine proteinase papain (inhibition constant = 10−5–10−4 m). The cDNA of the inhibitor was revealed to contain a 357-bp open reading frame encoding a 119-amino acid protein with a potential signal peptide (27 residues), indicating that this protein is synthesized as a preprotein and secreted outside the cells. Semiquantitative reverse transcription-polymerase chain reaction revealed that this gene expresses only in seeds, not in stems, leaves, and roots, suggesting that the protein is involved in seed development and/or germination. The inhibitor showed about 40% sequence homology with type-I nonspecific lipid transfer protein (nsLTP1) from other plant species. Actually, this inhibitor exerted both lipid transfer activity and lipid-binding activity, while the protein did not show any antifungal and antibacterial activities. Furthermore, the site-directed mutagenesis study using a recombinant ginkgo nsLTP1 revealed that proline (Pro)-79 and phenylalanine-80 are important on phospholipid transfer activity and that Pro-79 and isoleucine-82 are essential for the binding activity toward cis-unsaturated fatty acids. On the other hand, the α-helical content of P79A and F80A mutants was significantly lower than that of the wild-type protein. It was noteworthy that the papain-inhibitory activity of P79A and F80A mutants was elevated twice as much as that of the wild-type protein. In summary, we concluded that Pro-79 plays a critical role in both the lipid transfer and binding activities of ginkgo nsLTP1
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