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  • 1
    Electronic Resource
    Electronic Resource
    Energy transfer primers: A new fluorescence labeling paradigm for DNA sequencing and analysis (1996)
    [s.l.] : Nature Publishing Group
    Nature medicine 2 (1996), S. 246-249 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The ability to sequence DNA accurately and rapidly is revolutionizing biology and medicine. The confluence of the massive Human Genome Project, the sequencing of other bacterial and eukaryotic genomes, and the explosive growth of DNA sequence-based diagnostics is driving an increasing need for ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm0296-246
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  • 2
    Electronic Resource
    Electronic Resource
    Essentials extracted (1996)
    [s.l.] : Nature Publishing Group
    Nature 381 (1996), S. 290-290 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] MANY unrelated reasons prompt the chemical modification of peptides, proteins, oligonucleotides, sugars and poly-saccharides, lipids and glycolipids. The unifying elements are found in the chemical methods most commonly used and in the preferred (or most readily available) reagents. This book deals ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/381290a0
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  • 3
    Electronic Resource
    Electronic Resource
    Cryptomonad biliproteins — an evolutionary perspective (1995)
    Springer
    Photosynthesis research 46 (1995), S. 93-105 
    Details
    ISSN: 1573-5079
    Keywords: chloroplast evolution ; photosynthetic antennae ; serial endosymbiosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Each cryptomonad strain contains only a single spectroscopic type of biliprotein. These biliproteins are isolated as ≈50000 kDa αα'β2 complexes which carry one bilin on the α and three on the β subunit. Six different bilins are present on the cryptomonad biliproteins, two of which (phycocyanobilin and phycoerythrobilin) also occur in cyanobacterial and rhodophytan biliproteins, while four are known only in the cryptomonads. The β subunit is encoded on the chloroplast genome, whereas the α subunits are encoded by a small nuclear multigene family. The β subunits of all cryptomonad biliproteins, regardless of spectroscopic type, have highly conserved amino acid sequences, which show 〉 80% identity with those of rhodophytan phycoerythrin β subunits. In contrast, cyanobacteria and red algal chloroplasts each contain several spectroscopically distinct biliproteins organized into macromolecular complexes (phycobilisomes). The data on biliproteins, as well as several other lines of evidence, indicate that the cryptomonad biliprotein antenna system is ‘primitive’ and antedates that of the cyanobacteria. It is proposed that the gene encoding the cryptomonad biliprotein β subunit is the ancestral gene of the gene family encoding cyanobacterial and rhodophytan biliprotein α and β subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020420
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  • 4
    Electronic Resource
    Electronic Resource
    Cryptomonad biliproteins: Bilin types and locations (1996)
    Springer
    Photosynthesis research 48 (1996), S. 163-170 
    Details
    ISSN: 1573-5079
    Keywords: energy transfer ; light-harvesting pigments ; linear tetrapyrrole ; photosynthetic antennae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two crytophycean phycocyanins (Cr-PCs), Hemiselmis strain HP9001 Cr-PC 612 and Falcomonas daucoides Cr-PC 69 were purified and characterized with respect to bilin numbers, types and locations. Each biliprotein carried one bilin on the α subunit and three on the β subunit. Cr-PC 612 carried phycocyanobilin at α-Cys-18, β-Cys-82, and β-Cys-158, and a doubly-linked 15,16-dihydrobiliverdin at β-DiCys-50,61. Cr-PC 569 carried phycocyanobilin at α-Cys-18 and β-Cys-82, a singly-linked Bilin 584 at β-Cys-158, and a doubly-linked Bilin 584 at β-DiCys-50,61. This work, in conjunction with earlier studies on Cr-PE 545, Cr-PE 555, Cr-PE 566, and Cr-PC 645, shows that there is no conserved location for the bilin with longest wavelength visible absorption band among these proteins, and, consequently, that there is no conserved energy transfer pathway common to all native cryptophycean biliproteins. Only phycocyanobilin or phycoerythrobilin is found at β-Cys-82; there is greater bilin variability at the other three attachment sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00041006
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  • 5
    Electronic Resource
    Electronic Resource
    Transposon insertion in genes coding for the biosynthesis of structural components of the Anabaena sp. phycobilisome (1997)
    Springer
    Photosynthesis research 53 (1997), S. 109-120 
    Details
    ISSN: 1573-5079
    Keywords: cyanobacterium ; light-harvesting antenna ; phycobilisome ; phycobilisome linker polypeptide ; phycobiliprotein structural genes ; phycobiliprotein bilin lyase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Anabaena sp. PCC 7120 mutants defective in phycobiliprotein biosynthesis or phycobilisome assembly were generated by transposon mutagenesis. Four mutants with grossly reduced content of the major phycobiliprotein, phycocyanin, were found to have insertions within the cpcBACDEFG1G2G3G4 operon coding for phycocyanin biosynthesis and assembly. The insertion in mutant B646 separated the promoter from the open reading frames and eliminated production of the phycocyanin α (CpcA) and β (CpcB) subunits. Insertion in cpcC in mutant B642 eliminated production of the L36 Rlinker polypeptide required for assembly of phycocyanin into the distal discs of the phycobilisome rod substructures. Mutants B64328 and B64407 had insertions, respectively, in cpcE and cpcF, genes coding for the subunits of the heterodimeric lyase which catalyzes the attachment of phycocyanobilin to the phycocyanin apo-α subunit. Mutant SB12, often unable to survive under low light, was found to have an insertion in the apcE gene coding for the large core-membrane linker (L128 CM) that provides the scaffold for assembly of the phycobilisome core. DNA sequencing 3′ of apcE revealed genes apcABC, coding for the α and β subunits of allophycocyanin and for the small core linker L7.8 C. Amino acid sequence comparisons showed that the ApcA and ApcB proteins are 37% identical and that each of these polypeptides is highly similar to corresponding polypeptides from the distantly related filamentous strains Calothrix sp. PCC7601 and Mastigocladus laminosus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005816906539
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  • 6
    Electronic Resource
    Electronic Resource
    Microsatellite-based cancer detection using capillary array electrophoresis and energy-transfer fluorescent primers (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1742-1749 
    Details
    ISSN: 0173-0835
    Keywords: Cancer diagnosis ; Short tandem repeat ; Capillary electrophoresis ; Energy-transfer primers ; Microsatellites ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The development of sensitive, rapid, and accurate methods and apparatus for high-throughput short tandem repeat (STR) analysis will be critical for the use of microsatellite alteration in cancer screening. Here we show that STR-based bladder cancer diagnosis can be performed using capillary array electrophoresis and two-color labeling with energy-transfer (ET) fluorescent primers. Rapid (≤35 min) separations are achieved on capillary arrays using replaceable separation matrices and the allelic ratios are quantitatively determined with a precision of ± 10%. With this precision, a variation of 20% was considered diagnostically significant. These methods provide a significant improvement in the speed, ease, and precision of STR analyses compared to slab gel electrophoresis.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181007
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