{"title":"Transformation of Penicillium urticae with plasmids containing the hygromycin B resistance gene.","authors":"N. Kiuchi, A. Naruse, H. Yamamoto, J. Sekiguchi","doi":"10.1271/BBB1961.55.3053","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3053","url":null,"abstract":"A transformation system with efficiencies between 6 and 50 stable transformants per micrograms of DNA was developed for Penicillium urticae J1 (ATCC48163) using hygromycin B-resistant plasmids containing or not containing fragments of the P. urticae genome. The tandem repeated integration and/or random integration of vector DNA were observed. Although P. urticae was unable to grow in the presence of 200 micrograms/ml hygromycin B, the transformants were resistant to more than 5 mg/ml of hygromycin B.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"4 1","pages":"3053-7"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78532812","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. Yokogoshi, K. Hayase, J. Yamazaki, K. Koike, Shushichi Takahashi
{"title":"Effects of Administration of an Extract of Tu-chung Leaf (Eucommia ulmoides, Oliver) on Muscle Protein Synthesis in Mice","authors":"H. Yokogoshi, K. Hayase, J. Yamazaki, K. Koike, Shushichi Takahashi","doi":"10.1271/BBB1961.55.3133","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3133","url":null,"abstract":"oldest herbs known and, from ancient times, its medical uses -such as to strengthen the intestinal organs and heart, to provide vigor of spirit, to remove fatigue, to prevent aging, and to strengthen bone and muscleshave been noted in China.l) However, its precise metabolic effects were not clear. Several investigators have confirmed the hypotensive action of aqueous and ethanol extracts of Tu-chung bark in various animals.2~4) It was considered that the systemic arterial hypotension caused by the Tuchung extract was peripheral vasodilation by its direct action on vascular smooth muscle.4) Manyappreciably morpho-pharmacological changes were also observed by feeding a water extract of Tu-chung.5) Takahashi et al.6) reported that in white laying hens the average oviposition rate of the group given Tu-chung leaves was improved, and also the contents of protein and RNA in the liver and muscle were significantly higher than those of hens 3133","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"25 1","pages":"3133-3134"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81465057","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}
Young-Choon Lee, Y. Miyata, I. Terada, T. Ohta, H. Matsuzawa
{"title":"Involvement of NH2-terminal pro-sequence in the production of active aqualyson I (a thermophilic serine protease) in escherichia coli","authors":"Young-Choon Lee, Y. Miyata, I. Terada, T. Ohta, H. Matsuzawa","doi":"10.1080/00021369.1991.10857921","DOIUrl":"https://doi.org/10.1080/00021369.1991.10857921","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"29 1","pages":"3027-3032"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86144857","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 thermostable tryptophanase from an obligately symbiotic thermophile, Symbiobacterium thermophilum.","authors":"S. Suzuki, T. Hirahara, S. Horinouchi, T. Beppu","doi":"10.1271/BBB.56.84","DOIUrl":"https://doi.org/10.1271/BBB.56.84","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 degrees C for 20 min and the optimum temperature for the enzyme activity for 20 min reaction was 70 degrees 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 difference in the thermostability of these two enzymes. The purified enzyme catalyzed the degradation (alpha, beta-elimination) of L-tryptophan into indole, pyruvate, and ammonia in the presence of pyridoxal-5'-phosphate. The Km value for L-tryptophan was 1.47 mM. 5-Hydroxy-L-tryptophan, 5-methyl-DL-tryptophan, L-cysteine, S-methyl-L-cysteine, and L-serine were also used as substrates and converted to pyruvate. The reverse reaction of alpha, beta-elimination of this tryptophanase produced L-tryptophan from indole and pyruvate in the presence of a high concentration of ammonium acetate.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"112 1","pages":"3059-66"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80674767","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. C. Lee, Y. Miyata, I. Terada, T. Ohta, H. Matsuzawa
{"title":"Involvement of NH2-terminal pro-sequence in the production of active aqualysin I (a thermophilic serine protease) in Escherichia coli.","authors":"Y. C. Lee, Y. Miyata, I. Terada, T. Ohta, H. Matsuzawa","doi":"10.1271/BBB1961.55.3027","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3027","url":null,"abstract":"Aqualysin I is a heat-stable subtilisin-type protease produced by Thermus aquaticus YT-1. The precursor of aqualysin I consists of four domains: an NH2-terminal signal peptide, an NH2-terminal pro-sequence, a protease domain, and a COOH-terminal pro-sequence. In Escherichia coli cells harboring recombinant plasmid carrying the aqualysin I gene, proteolytic activity is obtained on treatment at 65 degrees C and mature enzyme is detected. In the case of mutant genes containing partial deletions in the NH2-terminal pro-sequence, no proteolytic activity was detected and the precursor protein was found to be unstable in E. coli. These results indicate that the NH2-terminal pro-sequence is required to produce the active enzyme by stabilizing the precursor structure. Amino acid substitutions in the conserved sequence of the NH2-terminal pro-sequence found among subtilisin-type proteases made the processing faster compared with the wild type.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"56 1","pages":"3027-32"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89230348","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":"Okaramine C, a New Insecticidal Indole Alkaloid from Penicillium simplicissimum","authors":"H. Hayashi, T. Fujiwara, Sawao Murao, M. Arai","doi":"10.1271/BBB1961.55.3143","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3143","url":null,"abstract":"14'-CH3 1.65 s. 1.52 s. insecticidal activity toward the 3rd instar larvae of silkworm upon oral administration. One of them, okaramine A (1),1>3) is a new type ofindole alkaloid with a seven-ring system, the other one, okaramine B (2),2'3) being a derivative with a eitht-ring system. Since we were interested in the unique structure of okaramines, we tried to determine if okaramines or similar compounds were produced by other strains. As a result, Penicillium simplicissimum AHU8402 showed activity almost equivalent to AK-40, the producing strain of okaramines.4) In this paper, we report the isolation and structural elucidation of the insecticidal constituents of AHU 8402. Froman acetone extract of mycelia and media of this strain, three insecticidal compounds were isolated. Twoof them were identified as okaramine A (1) and okaramine B (2), and the third one seemed to be a new congener, which was termed okaramine C (3). High-resolution El mass spectrometry of 3 established its molecular formula as C32H36N4O3. The 1HNMR(Table I) and 13C-NMR(Table II) spectra showed","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"68 1","pages":"3143-3145"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76797326","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. M. Kim, M. Hidaka, H. Masaki, T. Beppu, T. Uozumi
{"title":"NifA protein synthesized in vitro binds to the upstream activator sequence in the promoter of the Klebsiella oxytoca nifB gene.","authors":"Y. M. Kim, M. Hidaka, H. Masaki, T. Beppu, T. Uozumi","doi":"10.1271/BBB1961.55.3121","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3121","url":null,"abstract":"The nitrogen fixation (nif) genes of various bacteria are transcribed with an RNApolymerase modulated by the alternative activated by the NifA protein.1* Several analyses of the Klebsiella pneumoniae nifYL promoter2'3) showed that not only binding of the NifA protein to the upstream activator sequence integration host factor (IHF) to the promoter region was essential for completetranscriptional activation. Here we demonstrate the binding ofKlebsiella oxytoca NifA protein synthesized in vitro to the UASof ni/B promoter and the interaction of IHF with the nifB promoter. The NifA protein was synthesized by a coupled transcription and translation4* of an artificial nifA gene, whose expression wascontrolled by the promoter of the chlor-amphenicol acetyl transferase gene, on pNOA1015)using S30 extract of Escherichia coli MRE600purchased from Amersham. To assay its DNAbinding activity, this trans-lation mixture was directly incubated with a DNAprobe","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"2 1","pages":"3121-3"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73408300","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":"Regioselective modification of Lysine's amino groups by proteases.","authors":"H. Kitaguchi, M. Ono, I. Itoh, A. Klibanov","doi":"10.1080/00021369.1991.10857914","DOIUrl":"https://doi.org/10.1080/00021369.1991.10857914","url":null,"abstract":"The regioselectivity of six serine proteases for the amino groups of lysine was investigated. alpha-Chymotrypsin showed a preference for the alpha-amino group, although the selectivity can be varied 10-fold depending on the reaction medium. Subtilisin Carlsberg and other bacterial proteases were highly specific for the epsilon-amino group, regardless of the reaction medium: they were used as catalysts for the preparative synthesis of isopeptides in anhydrous tert-amyl alcohol.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"26 1","pages":"3067-73"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83728034","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}
M. Kirihata, T. Kaziwara, Y. Kawashima, I. Ichimoto
{"title":"An Efficient Synthesis of (±)-α-Kainic Acid Using a 3-HydroxyalIylglycine Derivative as a Common Building Block","authors":"M. Kirihata, T. Kaziwara, Y. Kawashima, I. Ichimoto","doi":"10.1271/BBB1961.55.3033","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3033","url":null,"abstract":"( + )-α-Kainic acid (1) was synthesized by starting from a building block, N-Boc-3-acetoxyallylglycine ethyl ester (2). The key intermediate, a methyl 4-[(tert-butoxycarbonyl)prenylamino]-5-hydroxy-2-pentenoate derivative (9), was prepared from 2 in eight synthetic steps. After converting 10 into a methyl ester (11), intramolecular ene-carbocyclization of 11 gave a pyrrolidine derivative (12), which was converted to 1 in a moderate yield.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"4 1","pages":"3033-3037"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88590101","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":"Optical resolution and biological activities of S-23121, a new cereal herbicide","authors":"M. Okamoto, R. Sato, E. Nagano, H. Nakazawa","doi":"10.1080/00021369.1991.10867925","DOIUrl":"https://doi.org/10.1080/00021369.1991.10867925","url":null,"abstract":"trolling many broadleaved weeds.1} Like Nphenylimide herbicide S-23142, in which the l-methyl-2-propynyl of S-23121 is substituted by 2-propynyl, S-23121 induces an abnormal accumulation of protoporphyrin IX, leading to lipid peroxydation.1} S-23121, having a chiral center at C-l in its chemical structure, is an optically active compound. Antipodes of bioactive chiral molecules are often thought to show quite different biological activity. It is, therefore, of great interest to know whether both enantiomers of S-23121 show similar","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"15 12 1","pages":"3151-3153"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86965932","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}