Abstract
The salt-soluble proteins of groundnut meal were fractionated by precipitation with (NH 4) 2SO 4 by increasing the (NH 4) 2SO 4 saturation in steps of 10%. The sharp separation into arachin and conarachin claimed by earlier workers was not achieved, as protein was precipitated at each stage from 20 to 100% saturation with (NH 4) 2SO 4. The fractions so obtained were examined by disc electrophoresis on polyacrylamide gel and the amino acid compositions were determined by ion-exchange chromatography. Differences in both electrophoretic pattern and amino acid composition were found. The protein precipitated by CaCl 2 solution was similar in yield, nitrogen content, electrophoretic pattern, and amino acid composition to the fraction precipitating at 10–20% (NH 4) 2SO 4 saturation. The main differences in amino acid composition of the various fractions precipitated by (NH 4) 2SO 4 were found in the amino acids cystine, methionine, and lysine, which increased with increase in (NH 4) 2SO 4 saturation. The electrophoretic pattern and amino acid composition of “conarachin” varied according to the method of preparation.
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