Studies on Peanut Proteins

Part V. Molecular dimension and subunit structure of conarachin I and II.

Abstract

Conarachin I was heterogeneous and consisted of three kinds of main protein, which possessed glycine, threonine and serine(1:1:1)as the N-terminal amino acids (DNP method). The average molecular weight was 17, 000(1.8S)by sedimentation-diffusion method. The average axial ratio was estimated 2.9 from the frictional ratio f/f₀=1.233 and 3.2 from the intrinsic viscosity [η]=0.043dl/g, assuming the molecule of a prolate ellipsoid of revolution with 30% hydration.
Conarachin II seemed to be consisted of five subunits having the average molecular weight of 38, 000, which possessed glycine, (iso-)leucine, aspartic acid and glutamic acid(2:1:1:1)as the N-terminal amino acids. The axial ratio of the monomer form(8.2S, M.W.180, 000)was estimated 5.5 from f/f₀=1.442 and 5.6 from[η]=0.073dl/g, and the dimer form (13.3S, 370, 000) 5.4 from f/f₀=1.433 and 5.1 from [η]=0.067dl/g.