Journal of marine biotechnology最新文献

筛选
英文 中文
Physiological changes in the juvenile euryhaline teleost, the tilapia Oreochromis hornorum, injected with E. coli-derived homologous growth hormone. 注射大肠杆菌衍生的同源生长激素对大盐硬骨鱼幼鱼的生理影响。
Journal of marine biotechnology Pub Date : 1998-08-01
Guillén, Lleonart, Agramonte, Morales, Morales, Hernández, Vázquez, Diaz, Herrera, Alvarez-Lajonchere, Hernández, de la Fuente J
{"title":"Physiological changes in the juvenile euryhaline teleost, the tilapia Oreochromis hornorum, injected with E. coli-derived homologous growth hormone.","authors":"Guillén,&nbsp;Lleonart,&nbsp;Agramonte,&nbsp;Morales,&nbsp;Morales,&nbsp;Hernández,&nbsp;Vázquez,&nbsp;Diaz,&nbsp;Herrera,&nbsp;Alvarez-Lajonchere,&nbsp;Hernández,&nbsp;de la Fuente J","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Growth is a complex process in fish. This study was designed to test the effect of different levels of recombinant tilapia growth hormone (tiGH) injected intraperitoneally in juvenile hybrid tilapia Oreochromis hornorum. Tilapia GH cDNA was cloned from hybrid O. hornorum tilapia. The mature protein was expressed in E. coli under regulation of the phage T7 promoter. The E. coli-derived tiGH was partially purified to 67% purity and, following renaturation, was shown to be biologically active in in vivo and in vitro assays. Recombinant tiGH stimulated extracellular matrix synthesis as shown by 35S-sulfate uptake in ceratobranchial cartilage explants. Zero, 0.1, 0.5 and 2.5 µg tiGH/g body weight (gbw) were injected in tilapia, and the effects on the growth-promoting action, hepatosomatic index (HSI), and mRNA insulin-like growth factor (IGF) induction were measured. A significant increase in the body weight (P < 0.05) and length (P < 0.01) was observed in tilapia receiving 0.5 µg tiGH/gbw. However, tilapia receiving 0.1 and 2.5 µg tiGH/gbw did not show an increase in body weight and length with respect to the control group receiving BSA injections. Binding sites for the recombinant tiGH were identified in the liver. Consistent with its somatotropic actions, the IGF mRNA induction was observed in the groups injected with 0.1 and 0.5 µg tiGH/gbw (P < 0.05). No significant increase in the HSI was detected in the injected groups when compared to the control group. These results demonstrated that the injection of biologically active E. coli-derived tiGH produces physiological changes in juvenile tilapia that ultimately resulted in a growth-promoting action only at a dose of 0.5 µg tiGH/gbw.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20617082","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}
引用次数: 0
Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine. 鲤鱼普通肌肉和肠道二肽酶的独特催化作用。
Journal of marine biotechnology Pub Date : 1998-08-01
Aranishi, Watanabe, Osatomi, Cao, Hara, Ishihara
{"title":"Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine.","authors":"Aranishi,&nbsp;Watanabe,&nbsp;Osatomi,&nbsp;Cao,&nbsp;Hara,&nbsp;Ishihara","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Although carp muscular and intestinal dipeptidases are metalloenzymes acting only on dipeptides, some structural and enzymatic differences occur between them. The present study verifies distinctive actions during dipeptide hydrolysis by these enzymes in terms of their kinetic characterization. The intestinal enzyme was differentially inhibited by EDTA and 1,10-phenanthroline, whereas these compounds induced a similar level inhibition of the muscular enzyme. The Km and Vmax values of both enzymes for l-leucine-glycine hydrolysis varied during incubations with 1,10-phenanthroline and EDTA, and the Km or Vmax values of the intestinal enzyme increased or remained the same with increasing concentrations of 1,10-phenanthroline, respectively. Analysis of the kinetic parameters indicated that Co2+ and Mn2+ had noncompetitive effects on the muscular enzyme and that a noncompetitive activation on the intestinal enzyme was stimulated by 1.5 mM of Mg2+ and with increasing concentrations of Mn2+. The muscular enzyme acted on a wide range of l-configuration dipeptides, whereas the intestinal enzyme acted only on a select range of dipeptides with a hydrophobic amino acid at the N-terminal position. The Kcat/Km values of both enzymes for dipeptide hydrolysis showed that highly hydrophobic dipeptides served as their preferential substrates. Other kinetic parameters demonstrated distinctive hydrolytic action of the two enzymes on these dipeptides: a strong affinity of the low catalytic rate muscular enzyme, and a weak affinity of the high catalytic rate intestinal enzyme.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20617084","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}
引用次数: 0
A novel marine Bacillus with multiple amino acid analog resistance and selenomethionine-dependent antibiotic productivity. 具有多种氨基酸类似物抗性和硒代蛋氨酸依赖抗生素生产能力的新型海洋芽孢杆菌。
Journal of marine biotechnology Pub Date : 1998-08-01
Imada, Hotta, Okami
{"title":"A novel marine Bacillus with multiple amino acid analog resistance and selenomethionine-dependent antibiotic productivity.","authors":"Imada,&nbsp;Hotta,&nbsp;Okami","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Amino acid analogs (AAA) were used as selective pressures for isolation of marine bacteria with novel physiological properties and as effecters for antibiotic production. Relatively small numbers of isolates were obtained from a minimal medium containing aminoethylcysteine (AC), 3,4-dehydroproline (DP), 5-methyltryptophan (MT), and selenomethionine (SM). These bacteria exhibited a high probability (68%) of antibiotic production in the presence of AAA, which was 10-fold higher than that (7%) in the absence of AAA. Among them, strain 14, obtained as the only SM-resistant and SM-dependent antibiotic (selenohomocystine) producer, was characterized for microbiological properties. It showed taxonomic properties falling into those of the genus Bacillus, required seawater for growth, and exhibited a high level (0.5 mM) of resistance to all the AAAs tested. Neither known Bacillus spp. nor other marine isolates showed such properties. Therefore, the strain 14 appears to be the first marine Bacillus strain with unique AAA resistance and AAA-dependent antibiotic productivity. The AAA-resistance-based strategy was thus demonstrated to be effective for isolation of novel bacteria as well as for screening for antibiotic production.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20618214","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}
引用次数: 0
Construction of a marine cyanobacterial strain with increased heavy metal ion tolerance by introducing exogenic metallothionein gene. 引入外源金属硫蛋白基因构建一株重金属耐受性增强的海洋蓝藻菌株。
Journal of marine biotechnology Pub Date : 1998-08-01
Sode, Yamamoto, Hatano
{"title":"Construction of a marine cyanobacterial strain with increased heavy metal ion tolerance by introducing exogenic metallothionein gene.","authors":"Sode,&nbsp;Yamamoto,&nbsp;Hatano","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A marine cyanobacterial strain with enhanced heavy metal ion tolerance was constructed by introducing an exogenous cyanobacterial metallothionein gene, smtA, from a freshwater unicellular cyanobacterium, Synechococcus sp. PCC 7942. An expression vector harboring the c-phycocyanin (cpc) promoter and cpc N-terminal region was constructed and smtA was inserted into its multiple cloning site. The marine cyanobacterium, Synechococcus sp. NKBG 15041c, was highly sensitive to the heavy metal ions present in the medium. However, the recombinant marine cyanobacteria harboring the expression vector with smtA could grow even in the presence of 4 µM of CdCl2, at which concentration the wild-type strain did not grow.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20618210","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}
引用次数: 0
Immunofluorescent detection of ice-ice disease-promoting bacterial strain Vibrio sp. P11 of the farmed macroalga, Kappaphycus alvarezii (Gigartinales, Rhodophyta). 养殖巨藻Kappaphycus alvarezii (Gigartinales, Rhodophyta)中冰冰病促生菌Vibrio sp. P11的免疫荧光检测
Journal of marine biotechnology Pub Date : 1998-08-01
Largo, Fukami, Adachi, Nishijima
{"title":"Immunofluorescent detection of ice-ice disease-promoting bacterial strain Vibrio sp. P11 of the farmed macroalga, Kappaphycus alvarezii (Gigartinales, Rhodophyta).","authors":"Largo,&nbsp;Fukami,&nbsp;Adachi,&nbsp;Nishijima","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A specific immunofluorescent probe consisting of polyclonal antibodies was developed to detect a marine bacterium, Vibrio sp. strain P11, which was found in a previous study to promote the ice-ice disease in the cultivated red macroalga, Kappaphycus alvarezii. The method involves a combined application of the fluorescent stains, 4',6-diamidino-2-phenylindole (DAPI) and the P11 PAbs, into a homogenized seaweed sample (<1 g wet wt), which is prediluted to make bacteria countable under an epifluorescence microscope without serious interference from autofluorescing algal debris. The algal tissue homogenate is then filtered through a 0.2-µm-pore size Nuclepore membrane filter, serving as a mounting pad, and viewed using alternating ultraviolet and IB excitation filters to detect total and specific bacteria, respectively, on the same microscopic field, at the same time. The immunofluorescent probe could be used as a valuable tool in studying the infection mechanism of the bacterium in the macroalga in vitro.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20618211","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}
引用次数: 0
Purification and characterization of a novel dipeptidase from carp ordinary muscle. 鲤鱼普通肌中一种新型二肽酶的纯化及特性研究。
Journal of marine biotechnology Pub Date : 1998-08-01
Aranishi, Watanabe, Osatomi, Cao, Hara, Ishihara
{"title":"Purification and characterization of a novel dipeptidase from carp ordinary muscle.","authors":"Aranishi,&nbsp;Watanabe,&nbsp;Osatomi,&nbsp;Cao,&nbsp;Hara,&nbsp;Ishihara","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A novel dipeptidase was purified to homogeneity from the crude extract of carp ordinary muscle with an increase in specific activity of 4041-fold and a 4% recovery rate. The enzyme was determined to have molecular weights of 54,000 after reduction and 106,000 without reduction, indicating that it is composed of two sulfide-linking molecules of subunit peptide chains of identical molar size. The optimum hydrolysis pH and temperature of the enzyme were evaluated by l-leucine-glycine to be pH 8.5 and 40 degreesC, respectively, and it was markedly stable in the weak alkaline region and at temperatures below 30 degreesC. Dipeptide hydrolysis of the enzyme was inhibited by metalloprotease inhibitors, sulfide-specific reagents, metal chelating reagents and reductants. In addition, sulfide-affinity bivalent metals potently inactivated the enzyme, while Mg2+ and Mn2+ activated it to different extents, and Mn2+ was also effective on the restoration of the nearly completely inactivated enzyme. The enzyme had a broad range of action on dipeptides that are composed of only l-amino acids, such as l-leucine, l-methionine, l-phenylalanine, and l-valine at the C-terminal and l-alanine, l-leucine, l-methionine, and l-valine at the N-terminal, but it had no catalytic action on dipeptides containing l-proline and d-amino acids, tripeptides, and peptide derivatives.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20617080","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}
引用次数: 0
Purification and identification of angiotensin I-converting enzyme inhibitors from the red alga Porphyra yezoensis. 红藻紫菜血管紧张素i转换酶抑制剂的纯化与鉴定。
Journal of marine biotechnology Pub Date : 1998-08-01
Suetsuna
{"title":"Purification and identification of angiotensin I-converting enzyme inhibitors from the red alga Porphyra yezoensis.","authors":"Suetsuna","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The potent part of the angiotensin I-converting enzyme (ACE) inhibitory activity from Porphyra yezoensis hydrolysate was fractionated by using ion-exchange and gel-filtration techniques. Oral administration of the most potent inhibitory fraction (SP-I fraction, 200 mg/kg) to spontaneously hypertensive rats (SHR) showed a hypotensive effect. Using octadecylsilano column chromatography, the SP-I fraction was further separated into several peptides with potent inhibitory activities. The amino acid sequences of ACE inhibitory peptides derived from Porphyra yezoensis were Ile-Tyr (IC50: 2.69 µM), Met-Lys-Tyr (7.26 µM), Ala-Lys-Tyr-Ser-Tyr (1.52 µM), and Leu-Arg-Tyr (5.06 µM).</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20617085","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}
引用次数: 0
Identification of a novel putative SINE sequence in a Salmo salar cosmid clone. Salmo salar cosmid克隆中一个新的假定SINE序列的鉴定。
Journal of marine biotechnology Pub Date : 1998-08-01
Lundin, Mikkelsen, Syed
{"title":"Identification of a novel putative SINE sequence in a Salmo salar cosmid clone.","authors":"Lundin,&nbsp;Mikkelsen,&nbsp;Syed","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A novel putative SINE sequence was found in a randomly selected cosmid clone of Salmo salar. The sequence (cSSML032Alu, GenBank accession number: L77085) was found to have 78% identity in 212 bp, with one Salvelinus namaycush AluI satellite sequence (GenBank accession number: U27096) and 69% identity in 197 bp, with another AluI satellite sequence from S. namaycush (GenBank accession number: U27091). Colony hybridization of cSSML032Alu to a salmon cosmid library indicated its dispersed presence in the genome, with a copy number in the range of a few thousand. Direct terminal repeats of nine bases and a potential poly(A) tail remnant identified in the S. salar cSSML032Alu sequence indicate a possible ancient retroposon unit.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20618216","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}
引用次数: 0
Characterization of lipolytic activity associated with a Vibrio species of bacterium isolated from fish intestines. 从鱼肠中分离出的一种弧菌的溶脂活性研究。
Journal of marine biotechnology Pub Date : 1998-08-01
Henderson, Millar
{"title":"Characterization of lipolytic activity associated with a Vibrio species of bacterium isolated from fish intestines.","authors":"Henderson,&nbsp;Millar","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cultures of a species of Vibrio isolated from fish intestines and known to synthesize the polyunsaturated fatty acid eicosapentaenoic acid (20:5n-3) were incubated with di-[1-14C]palmitoyl phosphatidylcholine to determine if lipolytic enzymes are produced by the bacteria. After two days of culture, most radioactivity was recovered in the phospholipids of the bacterial cells. When supernatants from cultures of the Vibrio were incubated with either di-[1-14C]palmitoyl phosphatidylcholine, 1-palmitoyl-2-[1-14C]linoleoyl phosphatidylcholine or 1-[1-14C]palmitoyl lysophosphatidylcholine almost all radioactivity was recovered in the free fatty acid fraction after 24 h. Only very small levels of radioactivity from di-[1-14C]palmitoyl phosphatidylcholine were recovered in diacylglycerols and phosphatidic acid. Over the same incubation period 61% and 5% of the radioactivity originally present in glycerol tri-[1-14C]oleate and cholesteroyl [1-14C]oleate, respectively, was released to free fatty acids. Soybean phosphatidylcholine and cod roe phosphatidylcholine, which differed in polyunsaturated fatty acid profile, were both hydrolyzed by culture supernatant. The results suggest that the Vibrio species examined produces a phospholipase B capable of hydrolyzing both intact phospholipids and lysophospholipids.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20618209","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}
引用次数: 0
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
相关产品
×
本文献相关产品
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信