Publications by authors named "Norihiko Okochi"

A ready-made dry medium method for coliform count, the Medi·Ca CC method, was compared to the Violet Red Bile Agar method (Bacteriological Analytical Manual, Chapter 4, Enumeration of Escherichia coli and the Coliform Bacteria, Section G) for nine raw foods from four food categories: raw ground pork, raw lamb, raw ground chicken, raw tuna fillet, raw salmon fillet, raw shrimp, fresh peeled banana, fresh cut pineapple, and fresh cut apple. The 95% confidence interval for the mean difference between the two methods at each contamination level for seven matrixes from all four categories fell within the range of -0.50 to 0.

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A ready-made dry medium method for aerobic count, the MediCa AC method, was compared to the AOAC Official Method 966.23, Microbiological Methods, for seven different heat-processed meat matrixes: cooked roast beef, Chinese barbecued pork (barbecued pork seasoned with honey-based sauce), bacon, cooked ham, frankfurter (made from beef and pork), and boiled and cooked pork sausage. The 95% confidence interval for the mean difference between the two methods at each contamination level for each matrix fell within the range of -0.

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An automated microarray diagnostic system for specific IgE using photoimmobilized allergen has been developed. Photoimmobilization is useful for preparing microarrays, where various types of biological components are covalently immobilized on a plate. Because the immobilization is based on a photo-induced radical cross-linking reaction, it does not require specific functional groups on the immobilized components.

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We made micropatterned vascular endothelial cells, which have a regular capillary tube-like structure, on a bioactive hydrogel matrix. We applied a stamping method to transfer micropatterned bovine aortic endothelial cells to a growth factor-reduced basement membrane matrix (Matrigel) and type I collagen gel. In this study, we addressed the issues of how to accelerate cell transfer and the effective factors in doing so.

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Lc-WT, the wild-type light chain of antibody, and Lc-Triad, its double mutant with E1D and T27aS designing for the construction of catalytic triad within Asp1, Ser27a, and original His93 residues, were displayed on the cell surface of the protease-deficient yeast strain BJ2168. When each cell suspension was reacted with BODIPY FL casein and seven kinds of peptide-MCA substrates, respectively, a remarkable difference in hydrolytic activities toward Suc-GPLGP-MCA (succinyl-Gly-Pro-Leu-Gly-Pro-MCA), a substrate toward collagenase-like peptidase, was observed between the constructs: Lc-Triad-displaying cells showed higher catalytic activity than Lc-WT-displaying cells. The difference disappeared in the presence of the serine protease inhibitor diisopropylfluorophosphate, suggesting that the three amino acid residues, Ser27a, His93, and Asp1, functioned as a catalytic triad responsible for the proteolytic activity in a similar way to the anti-vasoactive intestinal peptide (VIP) antibody light chain.

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