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Interaction of phytic acid with 11S and 2S proteins from rapeseed (Brassica napus L.)

✍ Scribed by Schwenke, K. D. ;Mothes, R. ;Borowska, J. ;Kozlowska, H.

Publisher: John Wiley and Sons
Year: 1986
Tongue: English
Weight: 113 KB
Volume: 30
Category: Article
ISSN: 0027-769X
DOI: 10.1002/food.19860300354

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✦ Synopsis

composed in every case of the 4 main protein zones. Under heating conditions, when a, and b, remain partially in solution, these two zones are weaker in the precipitate [4].

When the assumption is right that a, and pi form one protomer subunit in the quaternary structure one can conclude that this a,-b,-subunit is the most stable one. Nevertheless, its stability is not high enough for it to remain completely in solution.

A comparison of the results of SDS-PAC electrophoresis in the presence and in the absence of reducing agents points to the formation of a disulphide bridged intermediate (40000 g . mol-I) possibly composed of two /-chains.

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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