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  • 1
    Electronic Resource
    Electronic Resource
    A phytochrome regulated pea transcript encodes ferredoxin I (1987)
    Springer
    Plant molecular biology 8 (1987), S. 53-59 
    Details
    ISSN: 1573-5028
    Keywords: DNA sequence ; ferredoxin ; genomic organisation ; pea ; phytochrome ; Fd: ferrdoxin protein ; Fed: ferredoxin gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have sequenced the pea (cv. Alaska) cDNA clone pEA46 (16) and shown that it codes for ferredoxin I. This clone has previously been shown to correspond to a transcript whose levels are controlled by phytochrome (Kaufman et al. (1985) Plant Physiol. 78: 388–393; Thompson et al. (1983) Planta 158: 487–500). The deduced amino acid sequence includes part of an hydrophobic transit sequence that shows only very limited homology to that of Silene pratensis ferredoxin. Genomic blotting analysis indicates that ferredoxin I is encoded by one or two genes. A genomic clone (4601) has been isolated that contains the ferredoxin gene and at least 14 kb of flanking sequences.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00016434
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Predicted sequence and structure of a vegetative lectin in Pisum sativum (1992)
    Springer
    Plant molecular biology 18 (1992), S. 857-863 
    Details
    ISSN: 1573-5028
    Keywords: lectin ; legume ; pea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We report the predicted sequence of four vegetative homologues (Blec1,2,3 and 4) of the pea seed lectin. This study indicates that, in contrast to the single-copy pea seed lectin (Kaminski et al., Plant Mol Biol 9: 497–507, 1987), the pea vegetative lectin is transcribed by at least four members of a highly conserved multigene family whose members are only distantly related to the pea seed lectin at the primary amino-acid sequence level. For example, Blec1 shares only 38% amino-acid identity with the pea seed lectin. However, molecular homology modelling predicts that Blec1 probably forms a similar tertiary structure to the pea seed lectin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019200
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    Paper (German National Licenses)
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