{"title":"Effects of an Indonesian Medicinal Plant, Curcuma xanthorrhiza Roxb., on the Levels of Serum Glucose and Triglyceride, Fatty Acid Desaturation, and Bile Acid Excretion in Streptozotocin-induced Diabetic Rats","authors":"S. Yasni, K. Imaizumi, M. Sugano","doi":"10.1080/00021369.1991.10859947","DOIUrl":"https://doi.org/10.1080/00021369.1991.10859947","url":null,"abstract":"To study the beneficial effects of traditional Indonesian foods on sugar and lipid metabolism, streptozotocin-induced diabetic rats were fed on purified diets containing 5% of either cellulose as a control or four kinds of Indonesian plants. One of them, Curcuma xanthorrhiza Roxb., improved the diabetic symptoms such as growth retardation, hyperphagia, polydipsia, elevation of glucose and triglyceride in the serum, and reduction of the ratio of arachidonate to linoleate in the liver phospholipids. C. xanthorrhiza specifically modified the amount and composition of fecal bile acids. Significance of these findings was discussed in the light of the improvement of several diabetic symptoms.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"51 1","pages":"3005-3010"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90058286","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Rapid Detection of Yeast in Orange Juice by Enzyme-linked Immunosorbent Assay","authors":"Motonobu Yoshida, H. Maeda, Y. Ifuku","doi":"10.1271/BBB1961.55.2951","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2951","url":null,"abstract":"Antisera against native yeast of 6 species, Candida intermedia, C. parapsilosis, C. guilliermondii, C. Iambica, Crytococcus lamentii, and Rhodotorula rubra, were prepared for use as probes in an enzyme-linked immunosorbent assay (ELISA). These antisera reacted with yeast cell surface antigens that are thought to consist of protein moieties. The qross-reactivities between the antisera and yeast of 11 species were investigated by immunofluorescent and immunoblotting methods. It was shown that ELISA using the antiserum against C. intermedia or C. parapsilosis, is a valuable means of detecting yeast in orange juice. Yeast of more than 103 were capable of being detected by ELISA.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"126 1","pages":"2951-2957"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88657202","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Y. Matsubara, T. Yusa, A. Sawabe, Y. Iizuka, S. Takekuma, Y. Yoshida
{"title":"Structures of new cyclic peptides in young unshiu (Citrus unshiu Marcov.), orange (Citrus sinensis Osbeck.) and amanatsu (Citrus natsudaidai) peelings.","authors":"Y. Matsubara, T. Yusa, A. Sawabe, Y. Iizuka, S. Takekuma, Y. Yoshida","doi":"10.1271/BBB1961.55.2923","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2923","url":null,"abstract":"Four cyclic peptides were isolated from young unshiu (unripe fruit), orange and amanatsu peelings, and their structures were established on the basis of FAB-MS (CID method) and 2D-NMR spectroscopic data, and by chemical evidence. They were each found to consist of seven or eight amino acids.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"1 1","pages":"2923-9"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88676713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
S V Lobov, R Kasai, K Ohtani, O Tanaka, K Yamasaki
{"title":"Enzymic production of sweet stevioside derivatives: transglucosylation by glucosidases.","authors":"S V Lobov, R Kasai, K Ohtani, O Tanaka, K Yamasaki","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>For the purpose of improving sweetness and a further study on the structure-sweetness relationship of steviol glycosides, transglycosylation of stevioside by a variety of commercial glucosidases was investigated. It was revealed that two alpha-glucosidases gave glucosylated products. Transglucosylation of stevioside by Pullulanase and pullulan exclusively afforded three products, 13-O-[beta-maltotriosyl-(1----2)-beta-D-glucosyl]-19-O-beta-D-g luc osyl- steviol (1), 13-O-[beta-maltosyl-(1----2)-beta-D-glucosyl]-19-O-beta-D-glucosyl- steviol (2) and 13-O-beta-sophorosyl-19-O-beta-maltotriosyl-steviol (3). All of these products have already been obtained by trans-alpha-1,4-glucosylation of stevioside by the cyclodextrin glucanotransferase starch system, and 1 and 2 have been proven to be tasty and potent sweeteners. Transglucosylation of stevioside by Biozyme L and maltose afforded three new products, 4, 5 and 6, the structures of these compounds being elucidated as 13-O-beta-sophorosyl-19-O-beta-isomaltosyl-steviol (4), 13-O-[beta-isomaltosyl(1----2)-beta-D-glucosyl]-19-O-beta-D-glucosyl- steviol (5) and 13-O-[beta-nigerosyl-(1----2)-beta-D-glucosyl]-19-O-beta-D- glucosyl-steviol (6). A significantly high quality of taste was evaluated for 4.</p>","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","pages":"2959-65"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12541905","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Purification and properties of gamma-glutamyltranspeptidase from Bacillus subtilis (natto).","authors":"Y Ogawa, H Hosoyama, M Hamano, H Motai","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>To understand the mechanism by which gamma-polyglutamic acid (gamma-PGA) in the sticky material of natto was synthesized, we purified the gamma-glutamyltranspeptidase (gamma-GTP) (EC 2.3.2.2) from the culture broth of Bacillus subtilis (natto) to homogeneity. gamma-GTP was composed of two subunits with molecular weight of 45,000 and 22,000. The N-terminal amino acid sequence of light subunit was homologous with that of gamma-GTP from Escherichia coli. The optimum pH and temperature of activity were 8.5 and 60 degrees C. The enzyme was inactivated by incubation for 15 min at pH 8.0 and 55 degrees C, but little loss of the activity was detected at 40 degrees C. gamma-GTP used glutamine as a gamma-glutamyl donor and acceptor for gamma-PGA synthesis. Dipeptides were better gamma-glutamyl acceptors than free amino acids.</p>","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","pages":"2971-7"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12544581","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Synthesis and Insect Growth Regulatory Activity of 1,5-Disubstituted Imidazoles with Non-terpene Chains","authors":"E. Kuwano, T. Hisano, M. Eto","doi":"10.1271/BBB1961.55.2999","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2999","url":null,"abstract":"1-Isobutyl-5-(4-phenoxyphenyl)imidazole (KK-98), an inhibitor of juvenile hormone (JH) biosynthesis in the cockroach, and related imidazole compounds were evaluated against silkworm, Bombyx mori, for their activity to induce precocious metamorphosis. KK-98 induced precocious metamorphosis in the 4th instar larvae at high doses. Replacement of the 4-phenoxy group by a 3-phenoxy or 3-benzyloxy group on the benzene ring increased the activity. Among this series of compounds, 5-(3-benzyloxyphenyl)-1-isopropylimidazole (8) showed the highest activity. The induction of precocious metamorphosis by compound 8 was rescued by the simultaneous application of methoprene, a JH minie. When newly molted 3rd instar larvae were treated with a high dose of compound 8, a few larvae formed larval-pupal intermediates in the 3rd instar stage, which has not been formed by treating of any other imidazoles so far.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"46 1","pages":"2999-3004"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77424781","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
H. Inui, Hideto Kosaki, Yoshitaka. Uno, Keiko Tabata, S. Hirano
{"title":"Induction of Chitinases in Rice Callus Treated with Chitin Derivatives","authors":"H. Inui, Hideto Kosaki, Yoshitaka. Uno, Keiko Tabata, S. Hirano","doi":"10.1271/BBB1961.55.3107","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3107","url":null,"abstract":"(2ml), containing 20mg of the TV-acetylchitosan, l ml of 0. 1 Mcitric acid/0.2 M Na2HPO4 buffer, pH 3.0, and enzyme solution, with shaking at 37°C for 1hr, and stopped by addition of 1 ml of6.7% Na2WO4in 1/3N H2SO4. After centrifugation (1500 x g, 10min), reducing sugars in the supernatant were measured by a modification of Schales' method.11} One unit (U) is denned as the amount of chitinase which produces 1 /imol of reducing sugars as vV-acetyl-D-glucosamine per min under these conditions. For separation of chitinases, crude extract was brought to 80% saturation by addition of solid (NH4)2SO4 at 4°C, and the resultant precipitate dissolved in 20ml of 25mM imidazole/HCl buffer, pH 6.8, containing 1 mMEDTA. The solution was dialyzed against the same buffer and put onto a DEAE-cellulofine column (1.5 x 14cm), equilibrated with the same buffer. Chitinases were eluted with 50ml of the buffer and then with 400ml of a linear concentration gradient (0 to 0.3 m) of NaCl in the buffer. Gel nitration was done on a Sephadex G-75 column (1.5 x 76cm), equilibrated with 0.2m sodium phosphate buffer, pH 6.0. Bovine serum albumin (66 kDa), ovalbumin (45kDa), a-chymotrypsinogen A (bovine pancreas, 26","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"60 1","pages":"3107-3109"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74588949","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Seibun Suzuki, T. Hirahara, S. Horinouchi, T. Beppu
{"title":"Purification and Properties of Thermostable Tryptophanase from an Obligately Symbiotic Thermophile, Symbiobactevium thermophilum","authors":"Seibun Suzuki, T. Hirahara, S. Horinouchi, T. Beppu","doi":"10.1080/00021369.1991.10864611","DOIUrl":"https://doi.org/10.1080/00021369.1991.10864611","url":null,"abstract":"A thermostable tryptophanase was extracted from a thermophilic bacterium, Symbiobacterium thermophilum strain T, which is obligately symbiotic with the thermophilic Bacillus strain S. The enzyme was purified 21-fold to homogeneity with 19% recovery by a series of chromatographies using anion-exchange, hydroxylapatite, hydrophobic interaction, and MonoQ anion-exchange columns. The molecular weight of the purified enzyme was estimated to be approximately 210,000 by gel filtration, while the molecular weight of its subunit was 46,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which indicates that the native enzyme is composed of four homologous subunits. The isoelectric point of the enzyme was 4.9. The tryptophanase was stable to heating at 65°C for 20 min and the optimum temperature for the enzyme activity for 20 min reaction was 70°C. The optimum PH was 7.0. The NH2-terminal amino acid sequence of this tryptophanase shows similarity to that of Escherichia coli K-12, despite a great diffe...","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"170 1","pages":"3059-3066"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87756711","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Effects of Three Kinds of Dietary Nitrogen Sources on the Metabolic Fate of Tryptophan","authors":"K. Shibata, M. Onodera","doi":"10.1271/bbb1961.55.2945","DOIUrl":"https://doi.org/10.1271/bbb1961.55.2945","url":null,"abstract":"We have recently reported that the conversion ratio of tryptophan to nicotinamide [urinary excretion of (nicotinamide + N1-methylnicotinamide (MNA)+ N1-methyl-2-pyridone-5-carboxamide (2-Py) + N1-methyl-4-pyridone-3-carboxamide (4-Py) (μmol/day)/tryptophan intake during urine collection (μmol/day)] was changeable according to the kind of dietary nitrogen sources. In these experiments, we investigated whether the fate of tryprophan is changeable according to nitrogen sources or not. Weanling rats were fed with a diet low in nitrogen (1.1311% nitrogen) containing a suitable amount of nicotinic acid (6 mg/100 g of diet) for 17 days. Egg white (EW), egg white proteolysate-5 (EWP-5), and mixture of amino acids simulating the amino acid pattern of EWP-5 were used as dietary nitrogen sources. The urinary excretion of 5-hydroxyindole-3-acetic acid and the sum of nicotinamide and its metabolites in the group fed with the EWP-5 diet was the lowest, but, the excretion ratio of (2-Py + 4-Py)/MNA, which has been repor...","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"72 1","pages":"2945-2949"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89522265","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ken‐ichi Tanaka, Hisami Yamada, T. Yoshida, T. Mizuno
{"title":"Overproduction and rapid purification of the Escherichia coli histone-like protein, H-NS","authors":"Ken‐ichi Tanaka, Hisami Yamada, T. Yoshida, T. Mizuno","doi":"10.1271/BBB1961.55.3139","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3139","url":null,"abstract":"E. coli cells produce a set of small and usually basic DNA-binding proteins, which were collectively termed histone-like proteins because their biochemical properties were thought to resemble those of eukaryotic histone.1* Of the five such histone-like proteins so far characterized, H-NS (or HIa) is an abundant and neutral one, with an apparent molecular weight of 16,000. The gene for H-NS has recently been cloned, sequenced, and mapped at 27 min on the E. coli genetic map.2)3) Results of previous extensive genetic studies on H-NS suggested that the product of the hns locus is an important DNA-binding protein for both the function and the architecture of nucleoprotein complexes concerned in crucial biological processes.4) Another intriguing finding on a possible","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"53 1","pages":"3139-3141"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74867165","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}