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Phosphorylation of the 12S Globulin from Rapeseed ( Brassica napus L . ) by Phosphorous Oxychloride: Chemical and Conformational Aspects

✍ Scribed by Schwenke, Klaus Dieter; Mothes, Ralf; Dudek, Steffi; Görnitz, Eckhard

Book ID
126414483
Publisher
American Chemical Society
Year
2000
Tongue
English
Weight
256 KB
Volume
48
Category
Article
ISSN
0021-8561

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The structure of the 12 S globulin from
The structure of the 12 S globulin from rapeseed (Brassica napus L.)
✍ Schwenke, K. D. ;Raab, B. ;Plietz, P. ;Damaschun, G. 📂 Article 📅 1983 🏛 John Wiley and Sons 🌐 English ⚖ 756 KB

The 12 S globulin of rapeseed represents an oligomeric protein with a molecular weight of 300,000. It is composed of 6 subunits, which are arranged in a trigonal. antiprism with the point group symmetry 32 (D3). Each subunit contains smaller units (polypeptide chains) with molecular weights in the

Simplified isolation procedure for the 1
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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.

Isolation of the 12 S globulin from Rape
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✍ Schwenke, K. D. ;Raab, B. ;Linow, K.-J. ;Pahtz, W. ;Uhlig, J. 📂 Article 📅 1981 🏛 John Wiley and Sons 🌐 English ⚖ 543 KB

## Abstract An isolation procedure for the 12 S rapeseed globulin is described which includes precipitation by dialysis, purification using gel chromatography on Sephadex G‐200, and ion‐exchange chromatography on DEAE‐Sephadex A‐50. The isolated globulin represents a neutral protein with an isoele