{"title":"Segregated Intake of Protein-rich and -free Diets in Two Meals a Day; Its Effect on Growth and Vital Functions in Rats","authors":"K. Sugiyama, K. Iwami, F. Ibuki","doi":"10.1271/BBB1961.55.2979","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2979","url":null,"abstract":"Growing rats meal-fed for 4 weeks with a 20% or 40% casein diet in the morning (9:00–11:00) and a non-protein diet in the evening (19:00-21:00), or vice versa, were examined for growth and metabolic changes. A pair of groups given the 40% casein diet at one meal and the protein-free diet at the other meal, although becoming a little different from each other in growth, did not significantly differ from the control given only the 20% casein diet at the two meals. A pair of groups alternately given the 20% casein and protein-free diets, although excelling in protein efficiency ratio, were far inferior in growth to the groups given the 40% casein diet at either of the two meals. In any case, the rats with alternation of the diets sufficient and deficient in protein preferred the 20% or 40% casein diet to the protein-free one at whichever feeding time, and had a higher body weight gain when the casein diet was administered in the evening. The differences among these groups in protein intake throughout the exp...","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"7 1","pages":"2979-2985"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89016343","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. Miura, Tadao Saito, H. Kitazawa, T. Itoh, T. Inamoto
{"title":"Specific Adsorption of Immunoglobulin G1 in Bovine Colostrum on Sephadex and Its Mitogenic Activity on Mouse Splenocytes","authors":"M. Miura, Tadao Saito, H. Kitazawa, T. Itoh, T. Inamoto","doi":"10.1271/BBB1961.55.3103","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3103","url":null,"abstract":"Bovine colostrum immediately after parturition contains a high concentration ofimmunoglobulin (Ig) in which 95% or more are IgG type1} and it is important for the bovine neonate to establish passive immunity. It is also known that bovine colostrum contains various biologically active components. However, components that affect the growth of the cells involved in the immunesystem are not known. It is known that Concanavalin A (Con A) from jack beans (Canavalia ensiformis) agglutinates erythrocytes of various animal species2) and has mitogenic activity for mouse T lymphocytes.3) Con A has been isolated by a single affinity chromatography on Sephadex gel.4) In 1983, Shimada et al.5) have reported the specific binding of a part ofIg in bovine plasma to Sephadex. From the similar properties of Con A and bovine serum Ig with respect to binding to Sephadex, we suspected that certain bovine","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"15 1","pages":"3103-3105"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75122143","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 of Chiral Methyl Cucurbate and Its Analogs","authors":"J. Takehara, T. Oritani, K. Yamashita","doi":"10.1271/BBB1961.55.2939","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2939","url":null,"abstract":"Natural ( + )-(1R,2S,3S)-methyl cucurbate (1b) and the ( – )-δ-lactone of 3-epi-cucurbic acid (16) were synthesized from (+)-(1R,6S,7R)-bicyclo [4.3.0] non-3-en-7-ol (5). Asymmetric hydrolysis of the acetate (8) of ( ± )-5 with pancreatin gave optically pure the ( + )-(7R)-alcohol (5) and (–)-(7S)-acetate (8). An ozonolysis product of ( + )-5 was transformed to ( – )-16 and ( + )-(3S)-1b with inversion of the (7R)-hydroxyl group. Similarly, unnatural (–)-1b and (+)-16 were prepared from optically pure ( — )-5. The growth inhibitory activities of these synthesized chiral compounds toward lettuce seedlings were examined.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"36 5 1","pages":"2939-2944"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77519057","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":"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":"","DOIUrl":"","url":null,"abstract":"<p><p>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.</p>","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","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":"12541906","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":"10.1080/00021369.1991.10857909","DOIUrl":"https://doi.org/10.1080/00021369.1991.10857909","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"119 1","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":"77480534","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}
T. Kurisaki, K. Munemura, K. Kobayashi, Masakuni Yamamoto, Midori Hayashi, A. Nakamura, J. Magae, H. Kusakabe, M. Uramoto, K. Isono, K. Nagai, M. Yamasaki
{"title":"E-15, a Novel Polysaccharide Mitogen from Nocardia Specific for B Cells","authors":"T. Kurisaki, K. Munemura, K. Kobayashi, Masakuni Yamamoto, Midori Hayashi, A. Nakamura, J. Magae, H. Kusakabe, M. Uramoto, K. Isono, K. Nagai, M. Yamasaki","doi":"10.1271/BBB1961.55.2987","DOIUrl":"https://doi.org/10.1271/BBB1961.55.2987","url":null,"abstract":"A novel mitogen, E-15, which induced blastogenesis of mouse splenocytes, was purified from the culture filtrate of an actinomycete through ethanol precipitation, anion and cation exchange column chromatography, and gel filtration. The producing organism was identified as Nocar dia asteroides. Spectronic study demonstrated that it was a polysaccharide. Acid hydrolysis of E-15 yielded glucose and glucosamine. The active substance was eluted at the molecular mass between 90 kDa and 750 kDa on gel filtration.E-15 induced a mitogenic response of mouse splenocytes above 1 μg/ml and its potency of induction was superior to a lipopolysaccharide that is known to be a polyclonal B cell-specific mitogen. It showed no toxicity up to 100 μg/ml. The cell surface phenotypes of the blast cells induced by E-15 were analyzed by flow cytometry; they had surface immunoglobulins but no Lyt-2 antigen. Thus it was suggested that E-15 was a B-cell-specific mitogen.","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"58 1","pages":"2987-2991"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88656060","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. Lobov, R. Kasai, K. Ohtani, O. Tanaka, K. Yamasaki
{"title":"Enzymic Production of Sweet Stevioside Derivatives : Transglucosylation by Glucosidases(Organic Chemistry)","authors":"S. Lobov, R. Kasai, K. Ohtani, O. Tanaka, K. Yamasaki","doi":"10.1080/00021369.1991.10857912","DOIUrl":"https://doi.org/10.1080/00021369.1991.10857912","url":null,"abstract":"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 α-glucosidases gave glucosylated products. Transglucosylation of stevioside by Pullulanase and pullulan exclusively afforded three products, 13-O-[β-maltotriosyl-(1 → 2)-β-d-glucosyl]-19-O-β-d-glucosyl-steviol (1), 13-O-[β-maltosyl-(1 → 2)-β-d-glucosyl]-19-O-β-d-glucosyl-steviol (2) and 13-O-β-sophorosyl-19-O-β-maltotriosyl-steviol (3). All of these products have already been obtained by trans-α-1,4-glucosylation of stevioside by the cyclodextrin glucano-transferase 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-β-sophorosyl-19-O-β-isomaltosyl-steviol (4), 13-O-β-isomaltosyl(l → 2)-β-d...","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"25 1","pages":"2959-2965"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90554454","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":"","DOIUrl":"","url":null,"abstract":"<p><p>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.</p>","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","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":"12541908","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":"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":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"55 12","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":"12541911","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":"Energy Metabolism of a Psychrophilic Bacterium, Vibrio sp., and Escherichia coli B at Low Temperature","authors":"T. Oguma, T. Araki, S. Sagisaka","doi":"10.1271/BBB1961.55.3119","DOIUrl":"https://doi.org/10.1271/BBB1961.55.3119","url":null,"abstract":"","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"44 1","pages":"3119-3120"},"PeriodicalIF":0.0,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77660466","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}