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  • 1
    Electronic Resource
    Electronic Resource
    Coffee seeds contain 11S storage proteins (1999)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 105 (1999), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A legumin-like seed protein was purified from the endosperm of coffee (Coffea arabica L. cv. Colombia). In contrast to legumes, where efficient storage globulin extraction requires buffered saline solutions well above the acidic pKI of the globulins, coffee legumin is readily extracted with acidic aqueous buffers. The coffee legumin migrates like other 11S storage globulins in sucrose gradients. Subunits of coffee legumin have an apparent molecular mass of about 55 kDa after one-dimensional SDS-polyacrylamide gel electrophoresis in the absence of a reducing agent. In the presence of 2-mercaptoethanol, two polypeptides appear that have apparent molecular masses of 33 and 24 kDa. Two full-length cDNAs were generated from mRNA of developing seeds that were more than 98% homologous. They had open reading frames of 1 458 and 1 467 bp. Each encoded legumin precursors of 486 and 489 amino acids, respectively (Mr=54 136 and 54 818). Examination of a 5′ promoter region from a coffee legumin gene revealed a putative legumin-box. Genomic DNA from C. arabica was digested with six different restriction endonucleases. After separation of the fragments by electrophoresis, single discrete fragments on DNA blots hybridized strongly to a cDNA probe for the acidic chain. Other fragments that hybridized weakly with this probe were visible after hybridization at very low stringency. DNA from other species and commercially important cultivars that comprise the genus Coffea produced similar results. Immunocytochemical studies revealed that some legumin was detected in the cytoplasm in mature coffee seeds, but that the majority of it was in large storage vacuoles that accounted for most of the cell volume.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1999.105119.x
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  • 2
    Electronic Resource
    Electronic Resource
    Narbonin, a novel 2S protein from Vicia narbonensis L. seeds: cDNA, gene structure and developmentally regulated formation (1995)
    Springer
    Plant molecular biology 28 (1995), S. 61-72 
    Details
    ISSN: 1573-5028
    Keywords: biosynthesis ; gene structure ; narbonin ; recombinant protein ; 2S globulin ; seed storage protein ; Victa narbonensis L.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract cDNA and genomic clones encoding narbonin, a 2S globulin from the seed of narbon bean (Vicia narbonensis L.), were obtained using the polymerase chain reaction (PCR) and sequenced. The full-length cDNA as well as genomic clones contain a single open reading frame (ORF) of 873 bp that encodes a protein with 291 amino acids comprising the mature narbonin polypeptide (M r ca. 33 100) and an initiation methionine. The deduced amino acid sequence lacks a transient N-terminal signal peptide. The genomic clones do not contain any intron. No homology was found to nucleic acid and protein sequences so far registered in sequence data libraries. The biosynthesis of narbonin during embryogenesis is developmentally-regulated and its pattern of synthesis closely resembles that of typical seed storage globulins. However, during seed germination narbonin was degraded very slowly, indicating that it may have other function than storage protein. Southern analysis suggests the existence of a small narbonin gene family. Narbonin genes were also found in four different species of the genus Vicia as well as in other legumes such as Canavalia ensiformis and Glycine max. In Escherichia coli a recombinant narbonin was produced which yielded crystals like those prepared from narbonin purified from seeds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00042038
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