Biomedical subjects
Publications and source records attributed to K Oba.
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Lactate dehydrogenase [L-lactate: NAD oxidoreductase, EC 1.1.1.27] was isolated from sweet potato root tissues. Two species of the enzyme (isozymes I and II) were separated by DE-52 cellulose column chromatography from healthy, cut, and black-rot diseased tissues. Isozymes I and II were purified from healthy and diseased tissues, respectively. Reduction of pyruvate by NADH with either isozyme I or II was inhibited by pyruvate at high concentrations, by NAD+ and by several mononucleotides. Isozyme I was inhibited by a lower concentration of adenine nucleotide than isozyme II, and Km for pyruvate was increased markedly at acidic pH in the case of isozyme I, but only slightly in the case of isozyme II. The molecular weights of both isozymes were determined to be 150,000 and they were found to be charge isomers by polyacrylamide gel electrophoresis. The enzyme activity increased in response to infection by black-rot fungus but decreased in response to cutting.
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When sweet potato (Ipomoea batatas) root tissue was infected by Ceratocystis fimbriata, activity of the enzyme system from mevalonate to isopentenyl pyrophosphate, especially of pyrophosphomevalonate decarboxylase (EC 4.1.1.33), was increased in the noninfected tissue adjacent to the infected region, preceding the furano-terpene production in the infected region. Cutting and incubation of sweet potato slices did not produce furano-terpenes, and only slightly increased the activity of the enzyme system from mevalonate to isopentenyl pyrophosphate. The enzymic activity in diseased tissue was localized in the soluble fraction, and was higher in the tissue from the surface to a depth of about 5 mm with gradual decrease toward the inner part.Mercuric chloride (0.1%, w/v) and sodium dodecyl sulfate (1.0%, w/v) were utilized as model inducers of furano-terpenes and pyrophosphomevalonate decarboxylase. The mercuric chloride- or sodium dodecyl sulfate-induced response was inhibited by administration of cycloheximide to the discs together with the inducer immediately after disc preparation. When cycloheximide or blasticidin S was applied together with the inducer, to the discs 9 hours or more after disc preparation, the induction was not inhibited but rather stimulated.
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Pyruvate decarboxylase [2-oxo acid carboxy-lyase, EC 4.1.1.1] was isolated from sweet potato roots and was partially purified from healthy and diseased tissues. There was no appreciable difference in properties between the enzymes from healthy and diseased tissues. The molecular weight of the enzyme was found to be 240,000 by polyacrylamide gel electrophoresis. Since sodium dodecyl sulfate polyacrylamide gel electrophoresis gave a molecular weight of 60,000 for the monomeric form of the enzyme, it is likely that sweet potato pyruvate decarboxylase contains 4 single polypeptide chains. The optimal pH of the decarboxylation reaction was 6.1--6.6. The Lineweaver-Burk double reciprocal plot curved upward, and the Hill coefficient was more than 1, with low concentrations of pyruvate. The enzyme was localized in the cytosol fraction. The activity of the enzyme increased in response to black-rot fungus infection, but decreased in response to cutting.
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Ad4BP (or SF-1) is an essential transcriptional factor for steroidogenesis as well as for the development of the reproductive axis. We elucidated the structure of the human Ad4BP gene. The spliced variants of Ad4BP gene, ELP1 and ELP2 in mice, are unlikely to be present in humans since the analysis of the human gene revealed an in frame stop codon, 36-bp before the first ATG of Ad4BP. The promoter sequence of human Ad4BP, upstream of non-coding exon 1 was highly conserved, and E-box was also found to be essential for the transcription of human Ad4BP gene. During the process of the human Ad4BP gene cloning, we happened to obtain an Ad4BP-related gene, FTZ-F1beta which also belongs to the nuclear receptor family. We revealed cDNA structures of rat FTZ-F1beta, and found that rat has at least two types of FTZ-F1beta isoforms, which differ only by 21 amino acids length in the A/B domain. The tissue distributions of FTZ-F1beta in rat examined by RT-PCR, was found to be abundant in liver, pancreas, and gastrointestinal tracts. These results suggest that the physiological significance of FTZ-F1beta is different from that of Ad4BP.