Six chloroform/mcthanol-solubl¢ proteins from oat endosperm (Avena saliva) have been isolated and characterized by a purification procedure based on extraction with volatile solvents, followed by reversed-phase high performan~ liquid chromatography. Three of these proteins, with an assessed mol~ular weight of 25,000, 27,000 and 32,000 Da, respectively, have been identified by immunoblotting using ¢oeliac sere, as the major co¢liac serum leA-binding components of oat endosperm. The N-terminal amino acid sequence of these proteins indicates that they correspond to oh., 74, and 7a avenins, respectively. We have tentatively named them 'coeliac immunoreactive proteins'. Another chloroform/methanol oat component shows weak g-amylase inhibitory activity and exhibits strong homology (60% identity) at the N-tgrmin~ with the g-amylase inhibitor from ragi (Eleusilze coracana).