| First Author | Egorov TA | Year | 1994 |
| Journal | Eur J Biochem | Volume | 224 |
| Issue | 2 | Pages | 631-8 |
| PubMed ID | 7925380 | Mgi Jnum | J:20694 |
| Mgi Id | MGI:68769 | Doi | 10.1111/j.1432-1033.1994.00631.x |
| Citation | Egorov TA, et al. (1994) The complete amino acid sequence and disulphide bond arrangement of oat alcohol-soluble avenin-3. Eur J Biochem 224(2):631-8 |
| abstractText | We have elucidated the complete amino acid sequence of one of the avenin components, avenin-3, isolated from oat (Avena sativa L.), variety Narymsky 943. The sequence of the protein was determined by sequencing of CNBr and trypsin-generated peptides in combination with mass spectrometry. The protein is a single polypeptide chain, consisting of 201 amino acid residues with M(r) 23,252.8. The N-terminal amino acid residue of the protein is blocked with 5-oxoproline (pyroglutamic acid). All eight cysteine residues in avenin-3 are involved in disulphide bonds. The positions of these bonds were established by identification of a CNBr cleavage product of the intact avenin containing all the disulfide bonds (S-S core). Subsequent subdigestion of this S-S core allowed isolation of disulphide bonded peptides detected by differential reverse-phase HPLC before and after reduction. As a result, all four disulphides Cys50 Cys183, Cys58 Cys77, Cys84 Cys85 and Cys97 Cys191 were identified. Comparison of avenins with other prolamins demonstrates a high degree of similarity, which is especially pronounced around the cysteine residues. Avenins differ slightly from other prolamins in having unique N-terminal sequences and some differences in the repeated sequence motifs. |
