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The structure of the 12 S globulin from rapeseed (Brassica napus L.)

✍ Scribed by Schwenke, K. D. ;Raab, B. ;Plietz, P. ;Damaschun, G.

Publisher
John Wiley and Sons
Year
1983
Tongue
English
Weight
756 KB
Volume
27
Category
Article
ISSN
0027-769X

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✦ Synopsis

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 range of 18,500 to 31,000. The protein contains the following 4 polypeptide chains differing by their molecular weights in the

πŸ“œ SIMILAR VOLUMES

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. πŸ“‚ Article πŸ“… 1984 πŸ› John Wiley and Sons 🌐 English βš– 232 KB πŸ‘ 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.

Isolation of the 12 S globulin from Rape
Isolation of the 12 S globulin from Rapeseed (Brassica napus L.) and characterization as a β€œneutral” protein On seed proteins. Part 13
✍ Schwenke, K. D. ;Raab, B. ;Linow, K.-J. ;Pahtz, W. ;Uhlig, J. πŸ“‚ Article πŸ“… 1981 πŸ› John Wiley and Sons 🌐 English βš– 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