An Electrophoretic Investigation of Groundnut the Structure of Arachins A and B Proteins
نویسنده
چکیده
1. The proteins of the groundnut cotyledon have been fractionated and analysed by DEAE-Sephadex chromatography and acrylamide-gel electrophoresis. Seventeen components were detected. 2. A new method is described for the preparation of arachin, using calcium precipitation. The product contains at least 99% of arachin. 3. The theory of acrylamide-gel electrophoresis is developed and applied to the arachin system to predict the molecular weight of one sub-unit of arachin. 4. A variant form of arachin, arachin B, has been discovered. Of 81 nuts, 27 contained only arachin B, 53 contained both arachin A and B, and one contained arachin A only. This is almost certainly a polymorphism of arachin; this is the first example of polymorphism to be reported in plant proteins. 5. A combination of controlled denaturation, electrophoretic analysis, ultracentrifuge and Sephadex filtration data has shown that arachin A contains four different kinds of peptide chains (a, P, y and 8). Arachin B contains only P, y and 8 chains. 6. The most probable structure for arachin B, mol.wt. 330 000 form, is 8 P, 2 y and 2 8 chains, and for arachin A, 4 a, 4 Pi, 2 y and 2 8 chains. Arachin without ,B chains was not found. 7. The a and ,B chains have mol. wts. of about 35 000 and the y and 8 chains of about 10000. 8. Three N-terminal groups were found: the a and ,B chains both terminate in glycine; the y and 8 chains terminate in isoleucine and glutamic acid. 9. Arachin contains no carbohydrate. 10. Disulphide bonds are not important in arachin: there are none between the a, ,B, y and 8 chains. 11. The amino acid compositions of arachins A and B are very similar. Glutamic acid and aspartic acid residues are exceptionally frequent.
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