Abstract
The prolamins from wheat (gliadin), rye (secalin), barley (hordein) and oats (avenin) were extracted with 70% aqueous ethanol. Reversed-phase high-performance liquid chromatography (RP-HPLC) on C 18 -silica gel revealed clear differences in elution patterns. Crude avenin from the oat variety Flamingsregent was sepoarated by preparative scale RP-HPLC into thirty components. The amino acid compositions indicate that the first group of minor components (peaks 1–14) comprised non-avenin proteins. The second group (peaks 15–30) was the predominant group and corresponded to avenin proteins. These were classified into three subgroups differing mainly in the content of hydrophobic amino acids (Leu, Ile, Val, Phe). Within these groups, the avenins had similar compositions and differed only in the content of a few amino acids. Avenins appeared not to be related to the prolamins of other cereals on the basis of the amino acid composition data.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
