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Online-Ressource

Advances in Computer Games : Many Games, Many Challenges. (2003)

van den Herik, H. Jaap.

New York, NY :Springer,

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Schlagwort(e): Artificial intelligence-Congresses. ; Electronic books.

Materialart: Online-Ressource

Seiten: 1 online resource (394 pages)

Ausgabe: 1st ed.

ISBN: 9780387357065

Serie: IFIP Advances in Information and Communication Technology Series ; v.135

URL: https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=6525637

DDC: 794.8/1526

Sprache: Englisch

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Industrieraps - Biotechnologie II : Teilvorhaben: Gentechnische Steigerung des Ölsäuregehaltes in Raps ; Abschlußbericht, Berichtszeitraum: 01.01.1993 bis 30.06.1996 (1997)

Heinz, Ernst ; Schmidt, Hermann

[Hamburg : Univ., Inst. für allgemeine Botanik]

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Schlagwort(e): Forschungsbericht

Beschreibung / Inhaltsverzeichnis: Ziel des High-Oleic Projektes ist ein gentechnologischer Eingriff in die Fettsäuredesaturierung bei der Akkumulation von Triacylglycerienen in Rapssamen

Materialart: Online-Ressource

Seiten: 11 p. = 88 kB, text

Ausgabe: [Electronic ed.]

URL: https://edocs.tib.eu/files/e001/236594001.pdf

URL: https://edocs.tib.eu/files/e001/236594001l.pdf

Sprache: Deutsch

Anmerkung: Contract no.: BMFT/BMBF 0310528F , nIndex , Differences between the printed and electronic version of the document are possible

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3

Digitale Medien

Stepwise engineering to produce high yields of very long-chain polyunsaturated fatty acids in plants (2005)

Wu, Guohai ; Truksa, Martin ; Datla, Nagamani ; [weitere]

[s.l.] : Nature Publishing Group

Nature biotechnology 23 (2005), S. 1013-1017

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ISSN: 1546-1696

Quelle: Nature Archives 1869 - 2009

Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: [Auszug] Very long chain polyunsaturated fatty acids (VLCPUFAs) such as arachidonic acid (AA), eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) are valuable commodities that provide important human health benefits. We report the transgenic production of significant amounts of AA and EPA ...

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1038/nbt1107

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4

Digitale Medien

A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products (1998)

Jorasch, Petra ; Wolter, Frank P. ; Zähringer, Ulrich ; [weitere]

Oxford BSL : Blackwell Science Ltd, UK

Molecular microbiology 29 (1998), S. 0

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ISSN: 1365-2958

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Biologie , Medizin

Notizen: We have isolated the ypfP gene (accession number P54166) from genomic DNA of Bacillus subtilis Marburg strain 60015 (Freese and Fortnagel, 1967) using PCR. After cloning and expression in E. coli, SDS–PAGE showed strong expression of a protein that had the predicted size of 43.6 kDa. Chromatographic analysis of the lipids extracted from the transformed E. coli revealed several new glycolipids. These glycolipids were isolated and their structures determined by nuclear magnetic resonance (NMR) and mass spectrometry. They were identified as 3-[O-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-1,2-diacylglycerol, 3-[O-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-1,2-diacylglycerol and 3-[O-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-1,2-diacylglycerol. The enzymatic activity expected to catalyse the synthesis of these compounds was confirmed by in vitro assays with radioactive substrates. In these assays, one additional glycolipid was formed and tentatively identified as 3-[O-β-D-glucopyranosyl]-1,2-diacylglycerol, which was not detected in the lipid extract of transformed cells. Experiments with some of the above-described glycolipids as 14C-labelled sugar acceptors and unlabelled UDP-glucose as glucose donor suggest that the ypfP gene codes for a new processive UDP-glucose: 1,2-diacylglycerol-3-β-D-glucosyl transferase. This glucosyltransferase can use diacylglycerol, monoglucosyl-diacylglycerol, diglucosyldiacylglycerol or triglucosyldiacylglycerol as sugar acceptor, which, apart from the first member, are formed by repetitive addition of a glucopyranosyl residue in β (1→6) linkage to the product of the preceding reaction.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00930.x

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Digitale Medien

Uridine-diphospho-sulfoquinovose: diacylglycerol sulfoquinovosyltransferase activity is concentrated in the inner membrane of chloroplast envelopes (1998)

Tietje, Christine ; Heinz, Ernst

Springer

Planta 206 (1998), S. 72-78

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ISSN: 1432-2048

Schlagwort(e): Key words: Chloroplast envelope membrane ; Galactosyltransferase ; Sulfolipid ; 16:3/18:3 plants ; Sulfoquinovosyltransferase

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract. In experiments on the assembly of the sulfolipid sulfoquinovosyl diacylglycerol in envelope membranes of chloroplasts, UDP-sulfoquinovose (UDPS) was used with highest efficiency, and the corresponding enzyme, UDP-sulfoquinovose:diacylglycerol sulfoquinovosyltransferase, was partially characterized (E. Heinz et al., 1989, Eur J Biochem 184: 445–453). Here, we identified 35S- and 33P-labelled UDPS from various photosynthetically active organisms, suggesting that the sulfosugar nucleotide used for sulfolipid biosynthesis throughout the plant kingdom, including phototrophic bacteria, may indeed be UDPS. For attribution of the sulfolipid synthase to one of the two plastidial envelope membranes, these membranes were isolated from pea and spinach chloroplasts. The sulfoquinovosyltransferase was localized in the inner membrane of envelopes, which also contains the competing UDP-galactose:diacylglycerol galactosyltransferase. In contrast to the sulfoquinovosyltransferase, a substantial proportion of the galactosyltransferase was found in the outer membranes of envelopes from pea chloroplasts.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/s004250050375

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6

Digitale Medien

Cholesterol glucosylation promotes immune evasion by Helicobacter pylori (2006)

Churin, Yuri ; Winau, Florian ; Warnecke, Dirk ; [weitere]

[s.l.] : Nature Publishing Group

Nature medicine 12 (2006), S. 1030-1038

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ISSN: 1546-170X

Quelle: Nature Archives 1869 - 2009

Thema: Biologie , Medizin

Notizen: [Auszug] Helicobacter pylori infection causes gastric pathology such as ulcer and carcinoma. Because H. pylori is auxotrophic for cholesterol, we have explored the assimilation of cholesterol by H. pylori in infection. Here we show that H. pylori follows a cholesterol gradient and extracts the lipid from ...

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1038/nm1480

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7

Digitale Medien

Purification and cDNA sequencing of an oleate-selective acyl-ACP:sn-glycerol-3-phosphate acyltransferase from pea chloroplasts (1991)

Weber, Sabine ; Wolter, Frank -Peter ; Buck, Friedrich ; [weitere]

Springer

Plant molecular biology 17 (1991), S. 1067-1076

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ISSN: 1573-5028

Schlagwort(e): chilling sensitivity ; glycerolipid biosynthesis ; immunoscreening ; Pisum sativum ; tryptic sequences ; transit peptide

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract The soluble acyl-ACP:sn-glycerol-3-phosphate acyltransferase from chloroplasts of chilling-sensitive and -resistant plants differ in their fatty acid selectivity. Enzymes from resistant plants discriminate against non-fluid palmitic acid and select oleic acid whereas the acyltransferase from sensitive plants accepts both fatty acids. To use this difference for improving plant chilling resistance by biotechnology the gene for an oleate-selective enzyme is required. Therefore, the oleate-selective enzyme from pea seedlings was purified to apparent homogeneity. Tryptic peptides of internal origin were sequenced. Polyclonal antibodies raised in rabbits were used for an immunological screening of a pea leaf cDNA expression library in λgt11. A positive clone of 1800 bp was selected showing an open reading frame which codes for 457 amino acids. The deduced amino acid sequence coincides perfectly with the tryptic sequences. A tentative assignment of the processing site was made which divides the preprotein into a mature protein of 41 kDa in accordance with experimental findings and a transit peptide of 88 amino acids. At present the comparison between a selective (pea) and an unselective (squash) acyltransferase sequence does not provide a clue for recognizing the structural differences resulting in different selectivities.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00037145

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8

Digitale Medien

Brassica napus cDNAs encoding fatty acyl-CoA synthetase (1997)

Fulda, Martin ; Heinz, Ernst ; Wolter*, Frank P.

Springer

Plant molecular biology 33 (1997), S. 911-922

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ISSN: 1573-5028

Schlagwort(e): acyl-CoA ligase (AMP forming) ; AMP-binding protein ; enzymatic activity ; fatty acid ; northern blot ; sequence comparison

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract From a cDNA library of developing siliques of rapeseed (Brassica napus L.) we have isolated five full-length clones encoding polypeptides of the AMP-binding protein family. Two cDNAs encode fatty acyl-CoA synthetase activity (EC 6.2.1.3). The deduced polypeptides share about 52% identical amino acids. After expression in Escherichia coli the predicted enzymatic activity was confirmed by in vitro assays and product analysis. The enzymatic activity for one of the clones was characterized in detail by determination of the K m for oleic acid (10.4 µm) and the pH optimum (between 7 and 8). For the three additional clones no enzymatic activities could be demonstrated after expression in E. coli, although two of them exhibit similarity to either eukaryotic or prokaryotic acyl-CoA synthetases. The sequences are compared to a number of related expressed sequence tags from Brassica and Arabidopsis. Potential subcellular locations and functions of the deduced polypeptides within plant cells are discussed.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1023/A:1005780529307

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9

Digitale Medien

Purification and PCR-based cDNA cloning of a plastidial n-6 desaturase (1994)

Schmidt, Hermann ; Dresselhaus, Thomas ; Buck, Friedrich ; [weitere]

Springer

Plant molecular biology 26 (1994), S. 631-642

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ISSN: 1573-5028

Schlagwort(e): desaturase ; chloroplast envelope ; membrane protein purification ; reverse transcriptase/PCR ; transit peptide

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract A plastidial membrane-bound n-6 desaturase from spinach (Spinacia oleracea) was purified from chloroplast envelope membranes by anion exchange, cation exchange and ferredoxin-affinity chromatography. The molecular mass of the protein was estimated by SDS-PAGE to be 40 kDa. The highest specific activity of the desaturase in the final preparation was 196 nmol/min per mg protein with free oleic acid as the substrate. The N-terminal amino acid sequence of the blotted protein was determined and used for the construction of a degenerated and inosine-containing oligonucleotide primer for PCR experiments with cDNA transcribed from leaf mRNA. A 3′-RACE experiment with this primer amplified a single band of 1500 bp that after sequencing showed an open reading frame of 382 amino acids corresponding to a protein of 43 kDa. The 5′ end of the cDNA was amplified by a 5′-RACE experiment and isolated as a 500 bp fragment. Sequencing of this DNA revealed an additional 65 amino acids at the N-terminus of the native protein that are attributed to a plastidial leader peptide. With appropriate primers derived from these sequences a full-length clone was amplified by PCR and sequenced. Comparison of the plastidial oleate desaturase with the homologous enzyme from cyanobacteria showed about 50% amino acid homology. Comparison with other desaturases revealed three histidine boxes with the general sequence HXXXH that are highly conserved in all membrane-bound desaturases. These boxes might be involved in metal ion complexation required for reduction of oxygen.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00013749

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10

Digitale Medien

The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal -map and is a new member of the AMP-binding protein family (1994)

Fulda, Martin ; Heinz, Ernst ; Wolter, Frank P.

Springer

Molecular genetics and genomics 242 (1994), S. 241-249

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ISSN: 1617-4623

Schlagwort(e): FadD ; acyl-CoA synthetase ; AMP-binding ; Escherichia coli K12 ; Sequence

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: Abstract The fadD gene of Escherichia coli K12 was cloned and sequenced. The gene was identified by its ability to complement the corresponding mutant and by measuring the enzymatic activity after its expression in this mutant. The deduced polypeptide sequence exhibits similarity to other long chain acyl-CoA (coenzyme A) synthetases and a variety of other proteins, which together form a family of AMP-binding proteins. This family is extended by several new members and subdivided into four groups. fadD is assigned to a subgroup that does not include long chain acyl-CoA synthetases from eukaryotic organisms.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00280412

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