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":"","DOIUrl":"","url":null,"abstract":"<p><p>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.</p>","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","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":"12541904","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 Kobayashi, T Kamakura, T Tanaka, I Yamaguchi, T Endo
{"title":"Nucleotide sequence of the bsr gene and N-terminal amino acid sequence of blasticidin S deaminase from blasticidin S resistant Escherichia coli TK121.","authors":"K Kobayashi, T Kamakura, T Tanaka, I Yamaguchi, T Endo","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","pages":"3155-7"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12541912","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, T. Goda, S. Takase, M. Yamaguchi, T. Hoshi
{"title":"Effects of Suspension Hypokinesia/Hypodynamia on Ca Metabolism of Rats Fed with Various Protein Concentrations","authors":"H. Yokogoshi, T. Goda, S. Takase, M. Yamaguchi, T. Hoshi","doi":"10.1080/00021369.1991.10860085","DOIUrl":"https://doi.org/10.1080/00021369.1991.10860085","url":null,"abstract":"Hypokinesia/hypodynamia was induced in the hindlimbs of rats by a suspension harness, and metabolic balance studies, especially regarding calcium, were done. During a 10-day period of hypokinesia, the calcium concentration in the serum was not significantly altered with the exception of 5% casein diet, while the serum inorganic phosphorus concentration of hypokinetic rats was significantly decreased independent of the various dietary protein concentrations. Calcium balance in the suspended rats was significantly decreased, especially with the high protein diet, but the total calcium balance for 10 days was positive. The activity of alkaline phosphatase and the concentration of desoxyribonucleic acid (DNA) in the femoral diaphysis were markedly decreased by the suspension. These results demonstrate that the hypokinesia/hypodynamia by the suspension harness can induce a disorder of bone metabolism, and may be useful for studying the changes in bone metabolism caused by simulated weightlessness.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"43 1","pages":"3085-3089"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86655263","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 γ-Glutamyltranspeptidase from Bacillus subtilis (natta)","authors":"Y. Ogawa, H. Hosoyama, M. Hamano, H. Motai","doi":"10.1080/00021369.1991.10857918","DOIUrl":"https://doi.org/10.1080/00021369.1991.10857918","url":null,"abstract":"To understand the mechanism by which γ-poly glutamic acid (γ-PGA) in the sticky material of natto was synthesized, we purified the γ-glutamyltranspeptidase (γ-GTP) (EC 2.3.2.2) from the culture broth of Bacillus subtilis (natto) to homogeneity. γ-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 γ-GTP from Escherichia coli. The optimum pH and temperature of activity were 8.5 and 60°C. The enzyme was inactivated by incubation for 15 min at pH 8.0 and 55°C, but little loss of the activity was detected at 40°C. γ-GTP used glutamine as a γ-glutamyl donor and acceptor for γ-PGA synthesis. Dipeptides were better γ-glutamyl acceptors than free amino acids.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"9 1","pages":"2971-2977"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89793083","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":"Suppressive Effect In Vitro of Magnesium l-Ascorbyl-2-phosphate (APM), an Ascorbic Acid Derivative, on the Impairment of DNA by Glucose-6-phosphate","authors":"T. Ano, Akihiro Ohno, M. Shoda","doi":"10.1271/BBB1961.55.2967","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2967","url":null,"abstract":"We attempted to find compounds that suppress the DNA impairment caused by d-glucose-6-phosphate (Glc-6-P) by observing the loss of ability of pBR322 to transform Escherichia coli, and found that APM (magnesium l-ascorbyl-2-phosphate) suppressed the loss of transformability to less than 1/100 of that in the absence of APM. Wiien 2′-deoxyguanosine 5′-monophosphate (dGMP) was incubated in the dark with Glc-6-P and APM, changes in their absorbance patterns were observed, indicating possible suppression by APM of the interactions between dGMP and Glc-6-P. APM weakly suppressed the Maillard reaction.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"50 1","pages":"2967-2970"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89877657","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":"2-Keto-4-methylthiobutyric Acid in Urine of Rats Fed an Excess Methionine Diet","authors":"T. Kasai, Y. Ogo, Y. Otobe, S. Kiriyama","doi":"10.1271/BBB1961.55.3135","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3135","url":null,"abstract":"volved in those two Met metabolic pathways that excess Met is metabolized by the transsulfuration pathway3A) and that the limited capacity of this pathway is primarily responsible for the adverse effects of Met, at least on growth and food intake, probably resulting from its high level in the plasma and tissues.5) A direct NMRstudy provided support for the importance of Gly methylation, not transamination, in the catabolism of excess Met in rat liver.6) On the other hand, the quantitative importance of the transamination pathway remains unsolved.7) We have attempted to compare the patterns of components in plasma, various tissues, and urine of rats fed a low casein diet and a low casein diet supplemented with excess Met and proposed the pathway that OPA accumulated in the liver during sulfur-containing amino acids deficiency was used for the synthesis of GSHafter excess Met feeding, resulting in the decrease of OPAand increase ofGSHand a-ABA.8>9) This paper deals with the presence ofKMTBand HMTB,a transamination product of Met and its derivative, in urine of rats fed an excess Met diet and the significant decrease ofKMTBby addition ofGly to the excess Met diet.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"101 1","pages":"3135-3138"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79384067","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 M Klibanov","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>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.</p>","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","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":"12541909","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 Reaction Time and Temperature on the Formation of Volatiles from l-Cysteine and Propanal Heated in a Triglyceride–Water System","authors":"J. Okumura","doi":"10.1271/BBB1961.55.2931","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2931","url":null,"abstract":"The effects of reaction time and temperature on the volatile compounds formed from l-cysteine and propanal were studied in model systems heated in triglyceride–water (75:25). The volatile compounds, flavor profiles and yields formed in these model systems varied according to the reaction conditions. At 90 and 110°C, 2-methyl-2-pentenal was the most predominant component formed. Its maximum proportion occurred after heating for 1.5 hr at 110°C, and markedly decreased with temperatures over 110°C. 2-Ethylthiazolidine was the major product in the system heated at 140°C for 1.5 hr. 2-Ethylthiazolidino [3,4-b] thiazolidine could be detected in the system heated at 90°C for 1.5 hr. At 170°C, the profile of the volatile products was very complex, higher temperatures favoring the formation of nitrogen- and sulfur-containing compounds, including pyrrole, pyridines, thiophenes, thiazolidines, 1,2,4,-trithiolanes and 1,2,4-trithianes.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"65 1","pages":"2931-2937"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78707076","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":"Immobilization of Pseudomonas L-Phe oxidase on a nylon membrane for possible use as an amino acid sensor.","authors":"H Nakajima, H Koyama, H Suzuki","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","pages":"3117-8"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12541910","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. Tatsumi, S. Murakami, Y. Ogawa, A. Masaki, Y. Ishida, K. Murakami, H. Kawabe, H. Arimura, E. Nakano, H. Motai
{"title":"Autoproteolytic Processing and Processing-dependent Secretion of Aspergillus oryzae Alkaline Protease in Yeast","authors":"H. Tatsumi, S. Murakami, Y. Ogawa, A. Masaki, Y. Ishida, K. Murakami, H. Kawabe, H. Arimura, E. Nakano, H. Motai","doi":"10.1271/BBB1961.55.3099","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3099","url":null,"abstract":"visiae, directed the secretion of enzymatically active Alp into culture medium with its N-terminus identical to that of native Alp, demonstrating that the prepro region of 121 amino acids was processed correctly in the yeast.2) The deduced pre region of around 20 amino acids at the N-terminus of the prepro region is thought to be eliminated through translocation across the endoplasmic reticulum lumen by a signal peptidase, but it is not certain how the remaining pro region is processed. Two alternative mechanisms, autoproteolysis and the involvement of a processing enzyme, can be considered in the processing of proteases. With regard to the processing","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"3 1","pages":"3099-3101"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86787649","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}