{"title":"Antitumor glycogen from scallops and the interrelationship of structure and antitumor activity.","authors":"Takaya, Uchisawa, Ichinohe, Sasaki, Ishida, Matsue","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Hot water extract of scallop was treated with actinase E and fractionated by Sephadex G-25 gel-filtration and DEAE Sephadex A-25 ion-exchange chromatography. The antitumor activity of these fractions against Meth-A fibrosarcoma was examined. The nonadsorbed fraction (SCA25A) and weakly adsorbed fraction (SCA25B) obtained on DEAE Sephadex A-25 anion-exchange gel showed strong antitumor activity. Chemical analyses and NMR spectra identified SCA25A and SCA25B as glycogen. However, glycogen extracted from the scallop with trichloroacetic acid and from abalone showed no antitumor activity. This difference was thought to be due to variations in the fine structure of the glycogen molecule. The fine structure of glycogen was investigated by a sequential enzyme digestion method using beta-amylase and pullulanase, while the unit chain was analyzed by high performance anion exchange chromatography. The results showed that the antitumor active glycogen was highly branched with a shorter chain than glycogens without antitumor activity.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20762135","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":"Isolation of cDNAs for trypsinogen from the winter flounder, Pleuronectes americanus.","authors":"Douglas, Gallant","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Knowledge of the timing of digestive enzyme expression in developing larvae is essential for evaluating the appropriateness of formulated larval diets. Since little is known at the molecular biological level about the ontogeny of digestive enzyme function in flatfish, we have isolated cDNA clones for key digestive enzymes such as trypsinogen. Portions of trypsinogen genes have been amplified from winter flounder cDNA libraries by PCR using primers based on sequence motifs conserved among trypsinogen genes from other organisms. The PCR products were sequenced, cloned, and used as radioactively labeled probes to screen the libraries. Three distinct trypsinogen cDNAs have been isolated, representing the first cDNAs for winter flounder digestive enzymes. The first type (Flounder 1) is very similar to a trypsinogen sequence reported from a related flounder, Pleuronectes platessa. The second type (Flounder 2) is related to sequences reported from Atlantic salmon, cod, and the Antarctic fish, Paranotothenia magellanica. The third type (Flounder 3) shows limited similarity to the Antarctic fish trypsinogen sequence. All three cDNAs encode a cleavable signal sequence at the amino-terminal end, and Flounder 1 and 2 contain the characteristic acidic sequence for activation of the trypsinogen proenzyme to trypsin. Southern hybridization experiments indicate that Flounder 1 and 3 are single-copy genes, whereas Flounder 2 may be present in more than one copy. In addition, Flounder 2 detects homologs in a wide variety of other fish species. The sequence information will be used to establish RT-PCR assays for larval winter flounder (Pleuronectes americanus) digestive enzyme expression.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20762136","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}
Ramírez Orozco M, Hernández-Saavedra, Ascencio Valle F, Acosta González B, Ochoa
{"title":"Cell yield and superoxide dismutase activity of the marine yeast Debaryomyces hansenii under different culture conditions.","authors":"Ramírez Orozco M, Hernández-Saavedra, Ascencio Valle F, Acosta González B, Ochoa","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of aeration, pH, stirring rate, and temperature on the biomass production and superoxide dismutase (SOD) activity of the marine yeast Debaryomyces hansenii strain C-11 was determined. The cell biomass yield was approximately 50% in a seawater-formulated medium using glucose as the carbon source. The SOD activity increased by application of a pulse of oxygen or 0.8 mM sulfate copper into the chemical reactor. The SOD enzyme had an activity of 400 units/mg of protein in a crude extract produced under such conditions, the best activity ever reported for this enzyme in a crude preparation.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20762110","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":"An active Ac-like transposable element in teleost fish.","authors":"Hori, Suzuki, Inagaki, Oshima, Koga","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The i4/i4 genotype of the medakafish, Oryzias latipes, exhibits a quasi albino phenotype due to insertion of a novel transposable element, Tol2, into the tyrosinase gene. Tol2 is 4681 bp in length, has short inverted terminal repeats, and contains four ORFs with the potential to encode a transposase protein. Excision activity of the element has been detected by PCR analysis. Genomic Southern of the Tol2 element revealed that about 20 copies are present in the diploid genome. Dot-matrix comparisons of amino acid sequences of ORFs show relatively high similarity with transposases from Ac of maize, hobo of Drosophila, and Tam3 of snapdragon, which are all active transposable elements. Tol2 is thus concluded to be an active Ac-like transposable element probably encoding a transposase protein. It should therefore find application as a unique material for establishing a gene tagging system in fish.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20762133","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":"Nutrient regeneration in coastal seas by Noctiluca scintillans, a red tide-causing dinoflagellate.","authors":"Montani, Pithakpol, Tada","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Ammonium nitrogen, phosphate, and silicate contents in Noctiluca scintillans cell fluid were estimated at 2470, 183, and 54 pmol per individual, respectively. Ammonium nitrogen and phosphate concentrations at the surface layer of the water column seemed to be related to cell abundance of N. scintillans at the sampling location. Patches of N. scintillans provided 16 and 25 times greater concentrations of ammonium nitrogen and phosphate in the uppermost layer (0-10 cm depth) of the water column than those in the ambient seawater, respectively. Silicate concentration within patches, however, was close to that in surrounding water. The morphology of fecal pellets of N. scintillans fed on the diatom, Thalassiosira sp., was examined with a scanning electron microscope. The fecal pellet was composed entirely of visible structural diatom cells. It could be inferred that N. scintillans excretes silica from the diatom undigested in its fecal pellets and thus no remarkably high silicate concentration within red tide patches was observed.</p>","PeriodicalId":79672,"journal":{"name":"Journal of marine biotechnology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1998-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20762103","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":"Efficient rooting and acclimation of micropropagated Ruppia maritima Loisel.","authors":"Woodhead, Bird","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>An efficient protocol for rooting and acclimation of in vitro propagated Ruppia maritima was the focus of this research. The effects of four dilutions of a nutrient medium (f) and four different concentrations of sodium bicarbonate on rooting production were investigated. The optimal rooting medium was determined to be f/2 with 0.25 mM sodium bicarbonate in 5 ppt synthetic seawater at a pH of 7.5. Cultures of R. maritima were found to be photosynthetically inactive as measured by oxygen evolution in sucrose-based multiplication medium but were physiologically capable of adjusting to autotrophism once transferred to a bicarbonate medium. This transition was immediate and comparable to cultures that had acclimated in bicarbonate-based medium for 21 days. Ruppia maritima rooted onto coconut fiber mats and unanchored plants were acclimated in outdoor aquaria during May 1995. The results of these studies showed that micropropagated R. maritima can be acclimated easily and effectively at a low cost in aquaria, making R. maritima a useful seagrass species for restoration and mitigation projects.</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":"20617083","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":"A preliminary study of ribosomal DNA polymorphism in the tiger shrimp, Penaeus monodon.","authors":"Klinbunga, Penman, McAndrew","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The preliminary study of rDNA polymorphisms in P. monodon showed that inter- and intraindividual polymorphisms of rDNA were clearly observed in this species. Individual-specific rDNA restriction patterns were observed when digested with BamHI and SacI. The intergenic spacers (IGS) region of P. monodon rDNA plays an important role in length heteroplasmy at both between- and within-individual levels in this species.</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":"20618213","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":"Restriction-modification systems in the marine, aerobic, nitrogen-fixing unicellular cyanobacterium Cyanothece sp. ATCC 51142.","authors":"Soper, Hollister, Reddy","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cyanothece sp. ATCC 51142 possesses six host restriction-modification systems (HRMS), and these HRMS were designated as Csp68KI to Csp68KVI. So far, four restriction enzymes have been characterized biochemically, and the other two were deduced based on the cloning of corresponding DNA methyltransferase genes M. Csp68KIV and M. Csp68KV from the Cyanothece genome. Csp68KI, Csp68KII, Csp68KIII, Csp68KIV, Csp68KV, and Csp68KVI are isoschizomers of AvaII, AsuII, AvaIII, MspI, HaeIII, and FnuDII, respectively. The cleavage specificities for Csp68KI, Csp68KII, Csp68KIII, and Csp68KVI were characterized. The Cyanothece restriction enzymes showed different temperature and salt requirements for their optimal activity. For example, the restriction enzyme Csp68KII functions optimally at 50 degreesC and Csp68KIII requires higher salt for its activity.</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":"20618212","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":"Optimization of parameters for isolation of protoplasts from Gracilaria verrucosa (Rhodophyta).","authors":"Araki, Lu, Morishita","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A systematic method was designed for the isolation of a large number of protoplasts from an agarophyte alga Gracilaria verrucosa using agarase from a marine bacterium Vibrio sp. PO-303 and commercial enzymes (Cellulase Onozuka RS and Macerozyme R-10). Pretreatment of the tissue with 5% papain at 22 degreesC for 30 min before digestion with polysaccharide-degrading enzymes increased the protoplast yield. Suitable pH and temperature for the polysaccharide-degrading enzyme reaction were 6.5 and 22 degreesC, respectively. Mannitol (0.7 M) was found to be an excellent osmotic stabilizer. When the tissue (1 g, fresh wt.) of G. verrucosa pretreated with 5% papain solution (20 mM MES buffer, pH 7.5, containing 0.7 M mannitol) was digested with an enzyme mixture consisting of 4 units of agarase, 4% Cellulase Onozuka, 2% Macerozyme, and 0.7 M mannitol in 20 mM MES buffer (pH 6.5) with gentle agitation for 150 min at 22 degreesC, 1.03 x 10(8) protoplasts were obtained.</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":"20618215","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":"Quinolones from a bacterium and tyrosine metabolites from its host sponge, Suberea creba from the Coral Sea.","authors":"Debitus, Guella, Mancini, Waikedre, Guemas, Nicolas, Pietra","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A marine bacterium, identified as a pseudomonad, isolated from Suberea creba Bergquist, 1995 (Porifera, Dictyoceratida, Verongida, Aplysinellidae) collected along the eastern coast of New Caledonia, gave in culture phenazine-alpha-carboxamide, 2-n-heptylquinol-4-one, 2-n-nonylquinol-4-one, 2-n-(1'E-nonenyl)quinol-4-one, 3-n-heptyl-3-hydroxyquinolin-2,4-dione, a N-oxide-2-n-heptylquinoline derivative, and a benzyldiketopiperazine. None of these products could be detected, at the HPLC-UV sensitivity level, in the sponge extracts, which contained instead (+)-aerothionin, homoaerothionin, (+)-aeroplysinin-1, dibromo-, bromochloro-, and dichloroverongiaquinol. 2-n-Heptylquinol-4-one, (+)-aeroplysinin-1, and dibromoverongiaquinol showed strong antibacterial activity in vitro. The latter also proved promising for mariculture, rivaling chloramphenicol as an antibacterial agent in cultures of Pecten maximus larvae, while being nontoxic according to the Artemia salina test.</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":"20617081","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}