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Journal Article Effects of Idebenone on Cyanide-Resistant Respiration of the Mitochondria Isolated from Hansenula anomala Get access Nobuko Minagawa, Nobuko Minagawa Department of Biochemistry, Niigata College of Pharmacy, 5–13–2 Kamishin’ei-cho, Niigata 950–21, Japan Search for other works by this author on: Oxford Academic Google Scholar Noriyuki Takatsu, Noriyuki Takatsu Department of Pharmacochemistry, Niigata College of Pharmacy, 5–13–2 Kamishin’ei-cho, Niigata 950–21, Japan Search for other works by this author on: Oxford Academic Google Scholar Shigeru Sakajo, Shigeru Sakajo Department of Biochemistry, Niigata College of Pharmacy, 5–13–2 Kamishin’ei-cho, Niigata 950–21, Japan Search for other works by this author on: Oxford Academic Google Scholar Tadazumi Komiyama, Tadazumi Komiyama Department of Biochemistry, Niigata College of Pharmacy, 5–13–2 Kamishin’ei-cho, Niigata 950–21, Japan Search for other works by this author on: Oxford Academic Google Scholar Akio Yoshimoto Akio Yoshimoto Department of Biochemistry, Niigata College of Pharmacy, 5–13–2 Kamishin’ei-cho, Niigata 950–21, Japan Search for other works by this author on: Oxford Academic Google Scholar Agricultural and Biological Chemistry, Volume 55, Issue 3, 1 March 1991, Pages 845–846, https://doi.org/10.1080/00021369.1991.10870648 Published: 01 March 1991 Article history Received: 09 July 1990 Published: 01 March 1991
antibodies are required for the therapy of diseases to avoid undesirable side effects.9' Recently, we developed human-mouse hybridomas secreting human IgM class anti-ricin or anti-diphtheria toxin antibodies by the transformation of human peripheral blood lymphocytes (PBLs) with Epstein-Barr virus (EBV), followed by cell fusion between the transformed cells and mousemyelomaSP2/O2.10) With these hybridomas, we established hybrid hybridomas that secreted IgM class human bifunctional antibodies as a model experiment.ll' However, the affinity of the secreted hybrid IgM to diphtheria toxin was lower than that to ricin. One possibility for this is the low expression of immunoglobulin polypeptide genes to diphtheria toxin in the hybrid hybridoma, due probably to improper technique for the generation of the hybrid hybridoma. The previous method10' used actinomycin-D treatment of one hybridoma line to fuse with another 6-thioguanineresistant hybridoma line. Wesupposed that the actinomycin-D treatment in the fusion procedure were responsible for the lower affinity to diphtheria toxin of the produced bifunctional antibody, because Kobayashi et al. 12) reported that a T-cell hybridoma that had been generated by the actinomycin-D method tended to lose its capability of secreting some lymphokines. To solve this problem, we Fig. 1. Scheme for Generation of Hybrid Hybridoma Secreting Anti-neocarzinostatin/Anti-diphtheria Toxin Bifunctional Antibody.
An enzyme component that hydrolyzes pNP-G2 but not CMC has been isolated from a culture broth of Cellvibrio gilvus by a multi-step procedure involving Butyl-Toyopearl, DEAE-Toyopearl, and CM-Toyopearl chromatographies. The purified enzyme gave a single protein band on native, SDS-, and IEF-PAGE. The enzyme had a molecular weight of 40,000, an isoelectric point of 5.0, an optimum pH of 6.5, and an optimum temperature of 55 degrees C. It was stable from pH 4.0 to 9.0 at 37 degrees C for 1 hr and below 50 degrees C for 30 min. It hydrolyzed agluconic bonds not only of pNP-G2 but also of pNP-G3, pNP-G4, and pNP-G5. Cellooligosaccharides with D.P. of 3 to 5 were not hydrolyzed at all. Instead, the enzyme hydrolyzed xylan 4 times as fast as pNP-G2. Both HgCl2 and p-chloromercuribenzoic acid inhibited the two activities completely. Xylan inhibited the hydrolysis of pNP-G2 competitively. From these results, the purified enzyme was considered to be a unique xylanase that hydrolyzed the agluconic bonds of pNP-Gn.
Aminopeptidase C was purified from fresh chicken skeletal muscle by ammonium sulfate fractionation, and by successive chromatography on DEAE-cellulose, Ultrogel AcA 34, DEAE-cellulose again, and an alanine AH-Sepharose 4B affinity column twice. The purified enzyme migrated as a single band by SDS-PAGE. Aminopeptidase C was purified about 300-fold over the crude extract with a yield of 0.6%. The molecular weight of this enzyme was found to be 185,000 by gel filtration in a Sepharose 6B column and 92,000 by SDS-PAGE. The optimum pH for the hydrolysis of L-leucine beta-naphthylamide was 6.0-7.0, the enzyme being stable in the range of pH 6.5-8.0. The activity of this enzyme was strongly inhibited by EDTA and puromycin, and was high against the beta-naphthylamide derivatives of Lys, Leu, Ala and Met. The enzyme was more active towards tri- and tetrapeptides than towards dipeptides.
Thougha numberof proteinaceous cysteine proteinase inhibitors (cystatins) of animal origin have long been studied in detail,1* little is well-defined about plant cystatins except for oryzacystatins from rice seeds.2'3) Preceding the studies on oryzacystatins, however, we purified a cysteine proteinase inhibitor from corn.4'5) In this study we carried out amino acid analysis and kinetic studies on this inhibitor as a corn cystatin and also tried to comparethe results of the studies with those obtained with oryzacystatins. Inhibitory activities against cysteine proteinases were measured either by the method using benzoylarginine />-nitroanilide (BAPA)5) or by that using benzoylarginine /?-naphthylamide (BANA). Using the BANAmethod, inhibited proteinase activity was measured as follows: 0.1ml of 0.5m sodium phosphate buffer (pH 6.0)
Journal Article Isolation of Leu– Mutants and Transformation with YEpl3 Plasmid DNA in Saccharomyces exiguus Get access Taisuke Hisatomi, Taisuke Hisatomi Department of Biotechnology, Faculty of Engineering, Fukuyama University, Higashimura-cho, Fukuyama 729–02, Japan Search for other works by this author on: Oxford Academic Google Scholar Ei-ichi Inoue, Ei-ichi Inoue Department of Biotechnology, Faculty of Engineering, Fukuyama University, Higashimura-cho, Fukuyama 729–02, Japan Search for other works by this author on: Oxford Academic Google Scholar Yu-ichi Koubara, Yu-ichi Koubara Department of Biotechnology, Faculty of Engineering, Fukuyama University, Higashimura-cho, Fukuyama 729–02, Japan Search for other works by this author on: Oxford Academic Google Scholar Michio Tsuboi Michio Tsuboi Department of Biotechnology, Faculty of Engineering, Fukuyama University, Higashimura-cho, Fukuyama 729–02, Japan To whom correspondence should be addressed. Search for other works by this author on: Oxford Academic Google Scholar Agricultural and Biological Chemistry, Volume 55, Issue 4, 1 April 1991, Pages 1179–1180, https://doi.org/10.1080/00021369.1991.10870741 Published: 01 April 1991 Article history Received: 29 October 1990 Published: 01 April 1991
(1991). Structure of Mannan Fractionated from Water-soluble Mucilage of Nagaimo (Dioscorea batatas Dence) Agricultural and Biological Chemistry: Vol. 55, No. 9, pp. 2413-2414.
(-)-Capsaicinol, a natural antioxidant and an analog of capsaicin with no pungency, was synthesized from δ-valerolactone. The absolute stereochemistry of natural (-)-capsaicinol was derermined.
We have reported that the excretion ratio of nicotinamide metabolites, [N1-methyl-2-pyridone5-carboxamide (2-Py) + N1-methyl-4-pyridone-3-carboxamide (4-Py)]/N1-methylnicotinamide (MNA), is used as an index of amino acid adequacy. In this experiment, effects of protein-free diet feeding or starving on this excretion ratio were investigated using rats. The experimental period was 10 days. The urinary excretion of MNA, which is a major metabolites of nicotinic acid and nicotinamide, greatly increased with days, however, the urinary excretion of the MNA metabolites, 2-Py and 4-Py, decreased when rats were fed with a protein-free diet for 10 days. Accordingly, the resulting excretion ratio of (2-Py + 4-Py)/MNA in rats fed with the protein-free diet greatly decreased compared with that in rats fed with the 20% casein diet (control) (control vs. protein-free diet groups was 21.0 ± 3.5 vs. 0.5 ± 0.1 in urine samples on day 9-10). The urinary excretion of MNA did not increase when rats were starved for 10 days compared with that of the control. However, (2-Py + 4-Py)/MNA decreased to 3.6 ± 0.5 in urine samples on day 9-10. This decrease in the excretion ratio was attributed to the decrease in the activity of 2-Py- and 4-Py-forming MNA oxidase. These results further strengthen our claim that (2-Py + 4-Py)/MNA can be used as an index of amino acid adequacy.
