Abstract
THOUGH for most proteins there is a characteristic pH. range of stability to irreversible changes, seed proteins in general are particularly sensitive to mild conditions of acidity. Perhaps the classical example is the transformation edestin undergoes at a pH. of approximately 5, the so-called edestin-edestan transformation1. Conarachin was reported to undergo irreversible changes when exposed to pH values below 4 (ref. 2). This communication reports the effect of mild acidity on α-conarachin which is separated from the conarachin fraction of peanut proteins by chromatography on DEAE cellulose3. It is part of an investigation of the effect of acid conditions as a means of elucidating some of the structural aspects of seed proteins.
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EVANS, W., CARNEY, W. & NEUCERE, N. An Acid-induced Transformation of α-Conarachin. Nature 198, 1303–1304 (1963). https://doi.org/10.1038/1981303a0
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DOI: https://doi.org/10.1038/1981303a0
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