Reconstitution of conarchin from isolated subunits

Abstract

Conarchin II was isolated from peanut variety Type 25 and characterised. Seven subunits were isolated using PAGE and reconstitution of conarchin was studied. The reconstitution yield was greater than 90% and the reconstituted conarchin was identical in all respects with native protein. The weight ratio of the seven subunits was 1:1.1:1.3:1.8:1.4:15:16. The molecular weights and N-terminal amino acids of the isolated subunits were 75 000 and Val@ 1), 58 000 and Val (S 2), 50 000 and Pro (S 3), 40 000 and Val (S 4), 33 000 and Pro (S 5), 25 000 and Thr (S 6), 23 000 and Ala (S 7). No disulphide bonds were observed in the subunit association as protein dissociated into seven subunits in both the absence and the presence of 2-mercaptoethanol and SDS. The amino acid analysis of conarchin was conducted and the number of each residue was calculated.