You can manage bookmarks using lists, please log in to your user account for this.
Media type:
E-Article
Title:
The structure of the 12 S globulin from rapeseed (Brassica napus L.)
Contributor:
Schwenke, K. D.;
Raab, B.;
Plietz, P.;
Damaschun, G.
imprint:
Wiley, 1983
Published in:Food / Nahrung
Language:
English
DOI:
10.1002/food.19830270208
ISSN:
0027-769X;
1521-3803
Origination:
Footnote:
Description:
<jats:title>Abstract</jats:title><jats:p>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 (D<jats:sub>3</jats:sub>). 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 SDS‐electrophoresis; 18,500 ± 800, 21,100 ± 500, 26,800 ± 900, 31,200 ± 1,600. According to its quaternary structure the protein dissociates under milieu conditions.</jats:p><jats:p>The secondary structure of the protein is characterized by a low (11 %) content of α‐helix and a relatively high (31%) content of β‐conformation.</jats:p><jats:p>Owing to its structure and physico‐chemical properties the rapeseed protein is closely related to other 11/12 S globulins in the seeds of different plant species and botanical families.</jats:p>