Amino acid sequence of conglutin δ, a sulfur‐rich seed protein of Lupinus angustifolius L

FEBS Letters

Lilley, Glenn G.¹  Inglis, Adam S.¹ 

[1] CSIRO Division of Protein Chemistry, 343 Royal Parade, Parkville (Melbourne), 3052 Victoria, Australia

关键词: Legume storage protein (Lupinseed) Disulfide cross-link Free sulfhydryl group Sequence homology α-Amylase Enzyme inhibitor;   

DOI  :  10.1016/0014-5793(86)80167-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Complete amino acid sequences and disulfide cross-link arrangements have been determined for the two subunit polypeptides (M _r 9401 and 4597) ofconglutin δ, a helix-rich seed protein from Lupinus angustifolius cv. Uniwhite. There are two intrachain disulfide bonds and a free sulfhydryl group within the large chain and two interchain disulfide bonds to the small chain. The sequences show regions enriched in glutamineglutamic acid and serine residues which were correlated by a predictive method to the high measured level of α-helix (~ 38%). Homology was found between a cystine-rich region ofconglutin δ and the C-III α-amylase inhibitor from wheat suggesting that these proteins originated from a common ancestral gene.

【 授权许可】

Unknown