Abstract:Barley flour was defatted with petroleum ether and eliminated the salt and water soluble proteins with 2 times 5% NaCl and I time redistilled water extracting. After the above procedures, the hordein I was extracted with 55% isopropanol. The dry hordein I was solublized in 2% SDS and then separated by sephadex G-100 chromatography. The peak 2 hordein‘s molecular weight was 14–20 kD in SDS-PAGE protein pattern. Authors defined this group of hordein as hordein A. Its lysine content was 2.6%. The further experiments showed that this group of hordein A was soluble easily in isopropanol and alcohol but difficultly in 5% or 0.5 mol/l NaCl solution. It could be suggested that this group of hordein A is prolamine but not salt-soluble protein.