Publications by authors named "Manabu Fujiwara"

Nara sumi is a traditional Japanese craft that has been handed down in Nara since ancient times, and now plays a major role as a regional resource. Soot is considered to be one of the most important materials for its quality. However, the making process has been supported solely by the rule of thumb for craftsmen for many years, and there is very little scientific understanding of that.

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Germinal angiotensin I-converting enzyme (gACE) was purified to homogeneity from porcine seminal plasma. The molecular weight of the purified enzyme was calculated to be 182,000 on non-denaturing PAGE and 94,000 and 93,000 on SDS-PAGE in the absence and presence of beta-ME, respectively. These findings suggest that the enzyme is composed of two identical subunits in seminal plasma.

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The self-aggregation process of 3(1)-epimerically pure and mixed zinc methyl bacteriopheophorbides-d (ZMBPhes-d) was examined by stopped-flow technique. A 33(v/v)% tetrahydrofuran (THF) - water solution of ZMBPhe-d was rapidly mixed with a 7(v/v)% THF - water solution to form a chlorosome-type aggregate with a red-shifted Qy band around 700 nm. We observed a rapid autocatalytic aggregation in a subsecond time scale.

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Aqueous assemblies of zinc chlorins possessing a nonionic (oligo)oxyethylene, a cationic quaternary ammonium or an anionic sulfonate group were prepared in the presence of a synthetic surfactant. The nonionic zinc chlorin formed aggregates when admixed with a nonionic surfactant such as Triton X-100 to give a highly ordered oligomeric J-aggregate similarly as natural bacteriochlorophyll-c or d does in a chlorosome. In addition, the coassemblies of the cationic zinc chlorin with an anionic surfactant and of the anionic zinc chlorin with a cationic surfactant gave large oligomers of these chlorophyllous pigments.

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Legumain (asparaginyl endopeptidase) was purified to homogeneity from bovine kidneys. The molecular mass of the purified enzyme was calculated to be 34000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the presence of beta-mercaptoethanol. The enzyme rapidly hydrolyzed the substrate Z-Ala-Ala-Asn-MCA and was strongly inhibited by N-ethylmaleimide, p-chloromercuribenzene-sulfonic acid, Hg(2+) and Cu(2+).

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