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  • 1
    Electronic Resource
    Electronic Resource
    Proteolytic enzymes from recombinant Streptomyces lividans TK24 (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 65 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Different proteases from the culture fluids of recombinant Streptomyces lividans strains were isolated. Several individual proteases were separated and characterized. A chymotrypsin-chylike activity (CLA) was identified that specifically degrades a fusion protein between the α-amylase inhibitor from S. tendae (Tendamistat, HOE467) and proinsulin from the monkey Macaca fascicularis. The effective chemical inhibition of the degrading enzyme is demonstrated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03592.x
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  • 2
    Electronic Resource
    Electronic Resource
    High yield fermentation and purification of Tendamistat disulphide analogues secreted by Streptomyces lividans (1993)
    Springer
    Applied microbiology and biotechnology 38 (1993), S. 719-727 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In our studies of structure-function correlation of polypeptides we used Tendamistat (TM), an α-amylase-inhibitor of Streptomyces tendae, as a model to investigate the influence of different mutants on the expression and secretion of the protein. In addition, we examined the influence of replacing the two disulphide-bridges that stabilize the two-loop structure of the whole protein. The single mutants C27S, C27T, C45A, the double mutants C11A/C27A, C11A/C27S, C11A/C27T, C11A/C27L, C45/C73A and the fourfold mutant C11A/C27A/C45A/C73A were prepared. The mutated TM gene was expressed in S. lividans TK 24, which secretes the active form of the inhibitor into the culture medium. Compared with the wild-type, the double-mutated TM derivatives show an increase in secreted protein by a factor of two to ten. In contrast, the single-mutated inhibitor analogues show the reverse effect. In order to examine the influence of temperature and culture media on the production of protein derivative we used the most unstable C11A analogue. Our expression studies at 10, 19, 28 and 37° C established 19° C as the optimal temperature for production of the protein derivatives. The correlation between the stability and secretion of TM is discussed in the context of our knowledge of protein translocation in bacteria. Based on these experiments we optimized the fermentation parameters, isolated TM analogous on a large scale, and verified them.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00167134
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of disc-shaped phycobilisomes from the red alga rhodella violacea (1977)
    Springer
    Archives of microbiology 112 (1977), S. 61-67 
    Details
    ISSN: 1432-072X
    Keywords: Phycobilisomes ; Isolation methods ; Phycobiliproteins ; Accessory photosynthetic pigments ; Rhodella violacea ; Rhodophyceae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Disc-shaped phycobilisomes were purified from Triton X100 treated cell homogenates of the unicellular marine red alga, Rhodella violacea. Their absorption spectrum had principal maxima at 544 and 568 nm (B-phycoerythrin), 624 nm (C-phycocyanin) and a distinct shoulder at 652 nm (allophycocyanin). Intermolecular energy transfer within the phycobilisomes was clearly demonstrated by fluorescence data. Excited at 546 nm intact phycobilisomes showed a main fluorescence emission maximum at 665 nm, a minor one at 577 nm and a shoulder at 730 nm. Dissociated phycobilisomes revealed a composition of 58% B-phycoerythrin, 25% C-phycocyanin and 17% allophycocyanin under the cultural conditions used. Analytical methods resolved no other components than phycobiliproteins. In addition to the defined C-phycocyanin and two isoproteins of B-phycoerythrin a stable heterogeneous aggregate of B-phycoerythrin/C-phycocyanin was separated in considerable amounts. In the electron microscope negatively stained phycobilisomes appeared as elliptical aggregates having dimensions slightly above the values found in ultrathin sections and a detailed subunit structure. All observations and data suggest a new rhodophytan phycobilisome type in Rhodella violacea.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446655
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  • 4
    Electronic Resource
    Electronic Resource
    Isolierung und Charakterisierung der Biliproteide von Rhodella violacea (Bangiophycidae) (1974)
    Springer
    Archives of microbiology 100 (1974), S. 253-270 
    Details
    ISSN: 1432-072X
    Keywords: Phycobiliproteins ; Rhodophyceae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung 1. Die Zusammensetzung des Phycobiliproteidgehalts der einzelligen marinen Rotalge Rhodella violacea wurde untersucht. 2. Eine Methode zur Massenanzucht der Alge wird vorgestellt. 3. Die Isolierung und Reinigung der Phycobiliproteide aus Rohextrakten im Anschluß an die Ultraschallfraktionierung der Zellen erfolgte durch Gel- und Ionenaustauschchromatographie. 4. Das Vorkommen von B-Phycoerythrin, C-Phycocyanin und Allophycocyanin konnte für Rhodella violacea nachgewiesen werden. 5. Der hohe Reinheitsgrad der isolierten nativen Phycobiliproteide erlaubte ihre Charakterisierung durch Spektraldaten (Absorptionsspektren, Extinktionsverhältnisse und Fluorescenz-Emissionsspektren) und durch Bestimmung ihrer Molekulargewichte und isoelektrischen Punkte; die letzteren wurden mit 4,39, 4,46 und 4,79 für B-Phycoerythrin I, C-Phycocyanin bzw. Allophycocyanin ermittelt. 6. Die Phycobiliproteidkomposition unterscheidet Rhodella violacea deutlich von den Arten der Gattung Porphyridium und unterstützt damit die kürzlich vorgeschlagene Trennung von dieser Gattung.
    Notes: Abstract The phycobiliproteins of the unicellular marine red alga, Rhodella violacea, were investigated. A method of mass culture of the alga is presented. B-phycoerythrin, C-phycocyanin, and allophycocyanin were isolated from crude extracts by the combination of gel and ion exchange chromatography. The highly purified native phycobiliproteins were characterized by absorption spectra, absorption ratios, and fluorescence emission spectra, molecular weights, and isoelectric points. The latter were found to be 4.39, 4.46, and 4.79 for B-phycoerythrin I, C-phycocyanin, and allophycocyanin, respectively. The phycobiliprotein composition clearly distinguishes Rhodella violacea from Porphyridium aerugineum and P. cruentum, thus, supporting the separation of Rhodella violacea from the genus Porphyridium recently proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446322
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  • 5
    Electronic Resource
    Electronic Resource
    B-Phycoerythrin from Rhodella violacea (1975)
    Springer
    Archives of microbiology 104 (1975), S. 255-261 
    Details
    ISSN: 1432-072X
    Keywords: B-Phycoerythrin ; Isoprotein ; Phycobiliprotein ; Rhodella violacea ; Rhodophyceae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two isoproteins of the “native” B-phycoerythrin of the red alga, Rhodella violacea, were purified from crude extracts by preparative polyacrylamide gel electrophoresis and subsequently characterized. The slower moving pigment in gel electrophoresis was designated B-PE I, the faster as B-PE II. Both were found to occur in about equal amounts. B-PE I has a molecular weight of about 280000 and an IEP at 4.39, B-PE II a molecular weight of nearly 265000 and an IEP at 4.23. B-PE I and II are characterized by absorption maxima at 568 and 542 nm and a shoulder at 500 nm in the visible part of the absorption spectra. Their absorption coefficients at 542 nm differ with values of 5.54 and 5.63, respectively. The fluorescence emission spectra show a single maximum at 575 for B-PE I and at 578 nm for B-PE II. Both spectra have a shoulder at 630 nm. The fluorescence yield of B-PE II is lower by 25%. In calibrated SDS gel electrophoresis of the purified pigments B-PE I and II show two subunits of molecular weights of 18 900 and 29 200 and 18 500 and 29 900, respectively. Quantitative amino acid analyses indicated, that the isoproteins are very similar. B-PE II, however, has a significantly higher content of acidic amino acids and a lower percentage of basic residues, which is in keeping with its lower isoelectric point. Functional aspects of the occurrence of two isoproteins of B-phycoerythrin are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447334
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