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Isolation of a “neutral” 12 S globulin from rapeseed (Brassica napus L.)

✍ Scribed by Schwenke, K. D. ;Raab, B.

Publisher
John Wiley and Sons
Year
1979
Tongue
English
Weight
109 KB
Volume
23
Category
Article
ISSN
0027-769X

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Simplified isolation procedure for the 1
Simplified isolation procedure for the 12 S globulin and the albumin fraction from rapeseed (Brassica napus L.)
✍ Raab, Barbara ;Schwenke, K. D. 📂 Article 📅 1984 🏛 John Wiley and Sons 🌐 English ⚖ 232 KB 👁 1 views

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.

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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

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The polypeptide chain pattern of the rapeseed 12 S globulin i n the SDS gel electrophoresis is characterized by 4 main zones P X l , P E 2 , PpC3 and PPC4 with molecular masses of 18500, 21000, 27000 and 31000 D re8 ectively (1). Some of them split into double bands (Fig. ) 72). It wa8 suggested th