Simplified isolation procedure for the 12 S globulin and the albumin fraction from rapeseed (Brassica napus L.)
β Scribed by Raab, Barbara ;Schwenke, K. D.
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- English
- Weight
- 232 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0027-769X
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β¦ Synopsis
A simplified procedure for the isolation of chromatographic homogeneous albumin and 12 S globulin from rapeseed is proposed. The method includes prepurification of the proteins by means of fractionating precipitation and dissolution with ammonium sulphate and single chromatography on Sephadex G-200.
The most important advantages of the proposed technique are high yields of purified proteins and a simplification of isolation procedure by reducing the number of chromatographic runs.
π SIMILAR VOLUMES
## Academy of Sciences of the German Democratic Republic A reversible dissociation of the 12 S globulin from rapeseed (Brassica napus L.) depending on ionic strength (Short communication)
The influence of acylation on surface functional properties, solubility and heat-induced aggregation of the low-molecular weight basic protein fraction (napin) from rapeseed was studied. While the native protein was soluble over the whole pH-range, the exhaustively acetylated one became precipitable
The changes of some functional propertiessolubility, emulsifying and foaming properties, heat-induced aggregationof a native rapeseed globulin preparation after succinylation has been studied. In correspondence with the results obtained with the purified rapeseed 12 S globulin and other globulin pre
The 12 S globulin is an oligomeric storage protein in rapeseed with a molecular weight of 300 000 g . m1-l (1, 2 ) . Its molecular shape and quaternary structure has been investigated by means of small-angle X-ray scattering and by electron microscopy after negative staining (2 -4). The object