An Endogenous α-Amylase Inhibitor in Barley Kernels
- 1 July 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 72 (3), 809-812
- https://doi.org/10.1104/pp.72.3.809
Abstract
Barley (H. distichum cv. Klages) kernels contained a factor that converted malted barley .alpha.-amylase II to the .alpha.-amylase III form. After purification by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Sephacel and gel-filtration on Bio Gel P60, the factor gave a single band of protein on isoelectric focusing. The purified factor inhibited hydrolysis of soluble starch by .alpha.-amylase II from malted barley and germinated wheat (Triticum aestivum cv. Neepawa). .alpha.-Amylase I from these cereals was not affected. The inhibitor was not dialyzable and was retained by a PM 10 ultrafiltration membrane suggesting a MW > 10,000 daltons. Heat treatment of the inhibitor at 70.degree. C for 15 min at pH 5.5 and 8.0 resulted in considerable loss of inhibitory activity.This publication has 4 references indexed in Scilit:
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