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bertholletia/albuminas
Nuoroda įrašoma į mainų sritį
6 rezultatus
Mass spectrometry and structural characterization of 2S albumin isoforms from Brazil nuts (Bertholletia excelsa).
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Prisijungti Registracija
Proteomic approaches have been used to characterise the main 2S albumin isoforms from Brazil nuts (Bertholletia excelsa). Whilst most isoforms ( approximately 10 discrete protein species) exhibited molecular masses of around 12 kDa with a high amino acid sequence homology, important charge
Isolation, characterization and expression of a gene coding for a 2S albumin from Bertholletia excelsa (Brazil nut).
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Two genes, BE2S1 and BE2S2, coding for methionine-rich albumins of Brazil nut (Bertholletia excelsa H.B.K.) have been cloned and their sequence determined. The genes are members of a multigene family and one of them, i.e. BE2S1, codes for one of the dominant 2S isoforms. Its expression is highly
A chimeric gene encoding the methionine-rich 2S albumin of the Brazil nut (Bertholletia excelsa H.B.K.) is stably expressed and inherited in transgenic grain legumes.
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The coding region of the 2S albumin gene of Brazil nut (Bertholletia excelsa H.B.K.) was completely synthesized, placed under control of the cauliflower mosaic virus (CaMV) 35S promoter and inserted into the binary vector plasmid pGSGLUC1, thus giving rise to pGSGLUC1-2S. This was used for
Expression of the 2S albumin from Bertholletia excelsa in Brassica napus.
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The methionine rich 2S albumin seed storage protein of Bertholletia excelsa has been expressed in seeds of Brassica napus (rapeseed). A chimeric gene driven by the soybean lectin 5' flanking regions was used to produce a fusion protein consisting of the soybean lectin signal peptide and the
Purification and biochemical characterization of Brazil nut (Bertholletia excelsa L.) seed storage proteins.
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Brazil nut storage proteins, 2S albumin, 7S vicilin, and an 11S legumin, were purified using column chromatography. Analytical ultracentrifugation of the purified albumin, vicilin, and legumin proteins, respectively, registered sedimentation coefficients of 1.8, 7.1, and 11.8 S. Under reducing
The amino-acid sequence of the 2S sulphur-rich proteins from seeds of Brazil nut (Bertholletia excelsa H.B.K.).
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Storage proteins of the albumin solubility fraction from seeds of Bertholletia excelsa H.B.K. were separated by reversed-phase high-performance liquid chromatography and their primary structures were determined by gas-phase sequencing on intact polypeptides and on the overlapping tryptic and
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