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  • Articles  (2)
  • Cochlodinium polykrikoides  (1)
  • Tandemly Repeated DNA Cassette  (1)
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  • Articles  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of applied phycology 12 (2000), S. 191-193 
    ISSN: 1573-5176
    Keywords: algalytic activity ; α-mannosidase ; Cochlodinium polykrikoides ; dinoflagellate ; red tide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract α-D mannose is present on the surface of thetoxic dinoflagellate Cochlodinium polykrikoides.When exposed to the enzyme α-mannosidase, livecells of C. polykrikoides lost motility, roundedup, swelled gradually, and then lysed. The enzymedemonstrated a wide spectrum of lytic activity towardthe harmful algal species of the family Gymnodiniales,Alexandrium tamarense and Eutreptiellagymnastica, but showed less effect on useful feedalgae such as Chaetoceros calcitrans, Dunaliella salina, Isochrysis galbana, and Navicula pelliculosa.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0219-1032
    Keywords: Cleavable Linker Peptide ; Concatameric Peptide Multimers ; Peptide Analogs ; Tandemly Repeated DNA Cassette
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We designed a basic unit of the modified chicken gonadotropin releasing hormone II (cGnRH-II) peptide containing a trypsin cleavable linker peptide at both ends of the original peptide. We made a synthetic DNA coding for the modified cGnRH-II peptide with asymmetric and complementary cohesive ends of linker nucleotides. A tandemly repeated DNA cassette for the expression of concatameric short peptide multimers was constructed by ligating the basic units. The expressed peptide multimers were purified and subject to amino-terminal sequence analysis, which displayed the amino acid sequences expected from the designed nucleotides of the expression cassette. The monomeric cGnRH-II peptide analogs were generated after trypsin digestion. The present results showed that the technique developed for the production of the concatameric peptide multimers with cleavable linker peptides can be generally applicable to the production of short peptide analogs.
    Type of Medium: Electronic Resource
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