T. Mitsui, J. Fukami, K. Fukunaga, N. Takahashi, S. Tamura
{"title":"Studies on Piericidin","authors":"T. Mitsui, J. Fukami, K. Fukunaga, N. Takahashi, S. Tamura","doi":"10.1080/00021369.1970.10859740","DOIUrl":"https://doi.org/10.1080/00021369.1970.10859740","url":null,"abstract":"Respiratory inhibition by piericidin A was overcome by addition of vitamin K3 to the inhibited respiratory chain in mammalian mitochondria but not in insect mitochondria.Antagonistic effect of vitamin K3 on the inhibition of piericidin A was apparently found in respiration, blood pressure and heart rate in rat in vivo. Furthermore, toxicity of piericidin A to mouse and rat decreased when piericidin A was administered as the mixture of vitamin K3 in intraperitoneal route.No antagonistic effect of vitamin K3 was observed on the inhibition of piericidin A in TTC reaction of american cockroach nerve cord, femorals and digestive organs. Toxicity of piericidin A to some insects were not affected by vitamin K3.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"29 1","pages":"1101-1109"},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89015595","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":"Liquid Chromatography of Aflatoxins","authors":"M. Manabe, S. Matsuura","doi":"10.1080/00021369.1971.10859920","DOIUrl":"https://doi.org/10.1080/00021369.1971.10859920","url":null,"abstract":"There are numerous reports on studies of aflatoxins, but there are only a few reports on the isolation and mutual separation of aflatoxins by liquid chromatography. Following the previous reports on the liquid chromatography of four kinds (B1, B2, G1 and G2) of aflatoxins, the authors carried out the chromatography of six kinds of aflatoxins including aflatoxins B2a and G2a. Various kinds of adsorbents and eluting solvents were examined, and then the good mutual separation of aflatoxins was obtained by using the Sephadex G-10 (CM), a newly prepared adsorbent containing carboxymethyl group, and pure water for eluting solvent. Aflatoxins G2a, B2a, G2, B2, G1 and B1 were eluted in this order.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"43 1","pages":"417-423"},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83301776","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":"Non-foaming Mutants of Sake Yeasts","authors":"K. Ouchi, H. Akiyama","doi":"10.1080/00021369.1971.10860043","DOIUrl":"https://doi.org/10.1080/00021369.1971.10860043","url":null,"abstract":"Two selection methods of non-foaming mutants of sake yeasts (a kind of cell wall mutants lacking the ability to form froth head in sake mash) are described. The mutants, being different in both the affinity to gas bubble and in the agglutinability from the parent, were concentrated, by removing the wild type cells with froth in froth flotation method and by removing them by agglutination caused by lactobacillus cells in cell agglutination method. Spontaneous non-foaming mutants of Kyokai No. 7 strain were isolated from the concentrates after 9 successive trials of each selection procedure at the rates of 50% by the former and 81% by the latter. The UV-induced mutants were also isolated from the concentrates after the 7 successions at the rates of 80% and 100%, respectively, by the former and by the latter. There were two types among the non-foaming mutants with respect to the agglutinability; the one was non- or almost non-agglutinable type (type 1) and the other was weakly-agglutinable one (type 2). The ...","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"124 1","pages":"1024-1032"},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77459270","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":"Studies of the Peptide Antibiotic Suzukacillin","authors":"T. Ooka, I. Takeda","doi":"10.1080/00021369.1972.10860219","DOIUrl":"https://doi.org/10.1080/00021369.1972.10860219","url":null,"abstract":"Suzukacillin produced by Trichoderma viride 63Cl strain was purified and shown to be separated into two components A and B on thin-layer chromatography. The component A was isolated and crystallized from the mixture of components by alumina column chromatography. The component A is composed of six amino acids, Gly, Glu, Ala, Pro, Val, Leu and an unknown amino acid. This unknown amino acid was identified as α-amino isobutyric acid. It is supposed that α-amino isobutyric acid is biosynthesized mainly from l-valine by the isotopic experiments. Suzukacillin formation by Trichoderma viride 63Cl was stimulated by the addition of l-Asn, GABA, l-Ser, Gly and l-Arg into the medium.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"8 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84154710","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":"Studies on Colicin B","authors":"K. Arima, Yoshiki Katoh, T. Beppu","doi":"10.1080/00021369.1968.10859043","DOIUrl":"https://doi.org/10.1080/00021369.1968.10859043","url":null,"abstract":"The formation and the bactericidal action of colicin B, which had not been studied, were examined. When colicin B-producing cells were incubated with a low concentration of EDTA in water at 37°C for 30 min, almost all of colicins were extracted from cells into the surrounding medium. This technique was extremely effective for colicin I, which was not excreted into medium under usual conditions.Colicin B inhibited many macromolecular functions in the sensitive E. coli cells simultaneously, i.e., O2 uptake, oxidative phosphorylation, permeation activity for o-nitro-phenyl β-galactoside (ONPG) through cell membrane, and syntheses of protein, RNA and DNA.Colicin B could not be distinguished from colicin K by the cross-immunity test using K-colicinogenic strains. Colicin B had also many resemblances in the mode of action to colicine K, although their action was observed to be different in some points. These results indicated close relationship between colicins B and K.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"11 1","pages":"170-177"},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88670214","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":"Ruminal Fermentation and Sugar Concentrations","authors":"F. Hishinuma, S. Kanegasaki, H. Takahashi","doi":"10.1080/00021369.1968.10859234","DOIUrl":"https://doi.org/10.1080/00021369.1968.10859234","url":null,"abstract":"The maximal amounts of growth of Selenomonas ruminantium were examined in the media containing various amounts of glucose. The yields of cells per unit weight of glucose are linear functions to glucose concentrations in the ranges between zero to 0.005% and 0.005 to 0.7%, Cell yields per glucose are greater in the former range, indicating greater a-mounts of energy are available per glucose at lower concentrations. Growth responses in lactate media containing various amounts of glucose showed that the preincubation with larger amounts of glucose is inhibitory for the following growth and metabolism of lactate. The organism produces predominantly lactate in the glucose medium. However, volatile fatty acid productions increase when the initial concentrations of glucose become low. Isotopic studies showed that the lactate utilization yielding volatile fatty acids is inhibited by the preceding metabolism of high concentrations of glucose. These results were discussed with regard to normal and abnormal ferment...","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"220 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83700782","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":"Prodigiosin-25 C","authors":"Keiji Harashima, Nobuo Tsuchida, Junsaku Nagatsu","doi":"10.1080/00021369.1966.10858598","DOIUrl":"https://doi.org/10.1080/00021369.1966.10858598","url":null,"abstract":"A water-insoluble red antibiotic pigment was isolated from mycelia of a strain of Streptomyces. It was found that the pigment is a new C25-prodigiosin-analogue and the authors propose to designate it prodigiosin-25 C. The chemical structure (XI) has been deduced from visible absorption spectra, NMR spectra, mass spectra and analysis of degradation products of the pigment.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"94 1","pages":"309-310"},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77535467","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":"Anthocyanase and Anthocyanin Occurring in Eggplant (Solanum Melangena L.)","authors":"S. Sakamura, Susumu Watanabe, Y. Obata","doi":"10.1080/00021369.1965.10858372","DOIUrl":"https://doi.org/10.1080/00021369.1965.10858372","url":null,"abstract":"Experiments on anthocyanase and anthocyanin in eggplant were carried out by means of Warburg’s manometric method and determination of the anthocyanin. Results show that delphinidin 3-(p-coumaroylrutinoside)-5-glucoside from eggplant is oxidized by the polyphenol oxidase from mushroom, potato and eggplant flesh. The oxidative degradation of the anthocyanin is accelerated in the presence of chlorogenic acid which occurs in eggplant, and a mode of the action stimulating the degradation was discussed.In addition, an evidence was given that the existence of ascrobic acid in the enzymatic system retards the loss of the pigment, due to a coupled reaction, which is of well-known on the other o-dihydroxy phenols. Some observations on the product from the reaction mixture indicate that such decolorization of the anthocyanin progresses directly without hydrolysis of the glucosidic linkage.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"195 1","pages":"181-190"},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78993383","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":"Studies on the Water-Insoluble Enzyme","authors":"Hideo Suzuki, Y. Ozawa, H. Maeda","doi":"10.1080/00021369.1966.10858683","DOIUrl":"https://doi.org/10.1080/00021369.1966.10858683","url":null,"abstract":"Water-insoluble yeast invertase was prepared by binding native invertase to DEAE-cellulose. Some characteristics of the bound invertase and the continuous hydrolysis of sucrose by use of it are described. The activity of bound invertase corresponded to about 1/2 at pH 3.4 when compared with the maximum activity of free form and it could hydrolyze sucrose into invert sugar perfectly. The apparent optimum pH of bound invertase was shifted toward acid pH by about 2 pH units in comparison with free invertase. Stability of bound invertase to temperature was slightly less in comparison with free invertase at pH 5.2. The continuous sucrose hydrolysis was carried out using bound invertase at pH 3.6 and it could be used about ten times until the hydrolysis ratio decreased to the half of the initial.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"41 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75545008","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}
K. Hashizume, K. Kakiuchi, E. Koyama, Tokuji Watanabe
{"title":"Denaturation of Soybean Protein by Freezing","authors":"K. Hashizume, K. Kakiuchi, E. Koyama, Tokuji Watanabe","doi":"10.1080/00021369.1971.10859957","DOIUrl":"https://doi.org/10.1080/00021369.1971.10859957","url":null,"abstract":"When a solution of soybean acid-precipitated or 11S protein was frozen and stored at −1 to −5°C, the protein became partially insoluble after thawing. Ultracentrifugation and disc-electrophoresis of freeze-stored 11S protein solution after removing insoluble components revealed that new components which may be aggregates or associates of the 11S component were formed. When concentrated and stored at 5°C, disc-electrophoresis of 11S component showed that associates were formed. Mercaptoethanol could dissolve the insoluble protein and also convert the associates to the original 11S component. NEM–11S was not insolubilized by frozen storage at −5°C or storage at 5°C after being concentrated. From these facts it can be concluded that denaturation of soybean protein by freezing may be caused by intermolecular reactions through S-S bonds as a result of concentration by freezing. This may suggest a mechanism of the formation of sponge-like texture in kori-tofu which is made by frozen storage of soybean curd for ...","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"10 1","pages":"449-459"},"PeriodicalIF":0.0,"publicationDate":"2014-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78339562","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}
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