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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and characterization of prolyl hydroxylase from Chlamydomonas reinhardii (1986)
    Springer
    Planta 169 (1986), S. 238-244 
    Details
    ISSN: 1432-2048
    Keywords: Chlamydomonas ; Chlorophyta ; Prolyl hydroxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Prolyl hydroxylase, which is responsible for the hydroxylation of peptidyl proline residues, has been isolated and purified from the green alga Chlamydomonas reinhardii. The enzyme, which appears to be loosely associated with microsomal membranes, was released into solution by sonication in the presence of detergent. Purification was achieved by ion-exchange chromatography followed by affinity chromatography using the immobilized substrate poly-L-proline. Apart from its differing substrate specificity the enzyme appears to possess similar molecular characteristics to prolyl hydroxylase isolated from animal tissues: the active enzyme is a tetramer of about 240–250 kDa and nonidentical monomers of 65 and 60 kDa. The monomers are capsule shaped having a dimension of 12×7 nm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392320
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Legumin antibodies recognize polypeptides in coated vesicles isolated from developing pea cotyledons (1989)
    Springer
    Protoplasma 150 (1989), S. 79-82 
    Details
    ISSN: 1615-6102
    Keywords: Coated vesicle ; Intracellular transport ; Legumin precursor ; Cotyledons ; Pisum sativum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A highly enriched coated vesicle fraction has been isolated from cotyledons of developing pea seeds. This, and coated vesicles isolated from bovine brain as well as from bean leaves were subjected to SDS-PAGE followed by Western blotting with legumin antibodies. A distinct cross reaction with two polypeptides at around 60 kDa was seen, but only with the coated vesicles isolated from peas. Since legumin is synthesized as a 60 kDa precursor, but occurs as 40 and 20 kDa polypeptides in the protein body, we interpret our results as giving support to the idea that reserve proteins, like lysosomal proteins, are transported via coated vesicles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01403662
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The Endomembranes ofchlamydomonas reinhardii: A comparison of the wildtype with the wall mutants CW 2 and CW 15 (1986)
    Springer
    Protoplasma 133 (1986), S. 186-194 
    Details
    ISSN: 1615-6102
    Keywords: Chlamydomonas ; Endoplasmic reticulum ; Golgi apparatus ; Wall mutants ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ultrastructural observations on the principal endomembranes (endoplasmic reticulum, Golgi apparatus) of synchronously growing of wild type and mutant (CW 2, CW 15) strains ofChlamydomonas reinhardii have been carried out. The dictyosomes of the Golgi apparatus in all three cases are highly polar in morphology but lack intercisternal filaments. A clear spatial relationship between dictyosomes and endoplasmic reticulum is seen and a transfer of vesicles from the latter to the former is easily visualized. Coated vesicles invariably appear to be restricted to the trans-pole of the dictyosomes. The endoplasmic reticulum adjacent to the cis pole of dictyosomes is considerably hypertrophied in the case of the wild type, only partially so in the mutant CW 2 but not at all in the mutant CW 15. In the wild type this swelling is most extreme during the period of wall deposition and for several hours afterwards. The results are discussed in relation to the biosynthesis and intracellular transport of, particularly O-glycosidically linked, glycoproteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01304634
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Two polypeptides (30 and 38kDa) in plant coated vesicles with clathrin light chain properties (1988)
    Springer
    Protoplasma 146 (1988), S. 174-176 
    Details
    ISSN: 1615-6102
    Keywords: Clathrin light chains ; Coated vesicle ; Heat-stability ; Stains-all ; Zucchini
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Coated vesicles have been isolated from bovine brain and etiolated zucchini hypocotyls by centrifugal methods. By putting to use two properties of the light chain polypeptides of brain coated vesicles (calcium binding, heat stability) we have been able to demonstrate the presence of two similar polypeptides with apparent molecular masses of 30 and 38 kDa in plant coated vesicles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01405927
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    Paper (German National Licenses)
    Fulltext
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