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  • 1
    Electronic Resource
    Electronic Resource
    Precursors of one integral and five lumenal thylakoid proteins are imported by isolated pea and barley thylakoids: optimisation of in vitro assays (1993)
    Springer
    Plant molecular biology 23 (1993), S. 717-725 
    Details
    ISSN: 1573-5028
    Keywords: chloroplast ; precursor protein ; protein import ; thylakoid protein import
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In vitro assays for the import of proteins by isolated pea thylakoids have been refined and optimised with respect to (a) the method of thylakoid preparation, (b) the concentration of thylakoids in the import assay, and (c) the pH and temperature of the import assay. As a result, the 23 kDa and 16 kDa proteins of the photosynthetic oxygen-evolving complex are imported with efficiencies approaching 100%; import of the third oxygen-evolving complex protein is also observed, albeit with lower efficiencies. We have also demonstrated import of three further thylakoid proteins: plastocyanin, the CFoII subunit of the ATP synthase, and the photosystem I subunit, PSI-N, using this import assay. Import of plastocyanin, PSI-N and the 33 kDa oxygen-evolving complex protein subunit requires the presence of stromal extract whereas the other three proteins are efficiently imported in the absence of added soluble proteins. Import into isolated barley thylakoids was achieved under identical assay conditions, although with somewhat lower efficiency than into pea thylakoids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00021527
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  • 2
    Electronic Resource
    Electronic Resource
    The stromal processing peptidase activities from Chlamydomonas reinhardtii and Pisum sativum: unexpected similarities in reaction specificity (1993)
    Springer
    Plant molecular biology 23 (1993), S. 1291-1296 
    Details
    ISSN: 1573-5028
    Keywords: Chlamydomonas reinhardtii ; chloroplast ; protein import ; proteolytic processing ; thylakoid proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have partially purified the stromal processing peptidase from Chlamydomonas reinhardtii and compared the properties of this activity with those of the pea counterpart. Whereas previous studies have suggested that the two enzymes may have significantly different reaction specificities, we find that they are in fact very similar. Both enzymes process precursors of two higher-plant thylakoid lumen proteins, and one C. reinhardtii lumenal protein, to similar intermediate-size forms. However, whereas the algal enzyme processes the precursor of C. reinhardtii Rubisco small subunit to the correct mature size, this precursor is cleaved only to an intermediate size by the pea enzyme. The small subunit precursor from pea appears to be cleaved by both enzymes in a similar manner. In terms of sensitivity to inhibitors, the two activities are notably different; the pea enzyme has previously been shown to be inhibited by several types of heavy-metal chelator, but we have found that none of these compounds affect the algal activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00042363
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    Paper (German National Licenses)
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