Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily

FEBS Letters

Egorov, T.A.²  Shewry, P.R.¹  Odintsova, T.I.³  Musolyamov, A.Kh.²  Fido, R.¹  Tatham, A.S.¹ 

[1] IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS18 9AF, UK;Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilova Str., Moscow 117984, Russian Federation;Vavilov Institute of General Genetics, Russian Academy of Sciences, 3 Gubkina Str., Moscow 117809, Russian Federation

关键词: Seed;    Cereal;    Sunflower;    Wheat;    Albumin;    Inhibitor;    Gliadin;    Disulfide bond;   

DOI  :  10.1016/0014-5793(96)01117-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Disulphide mapping of a methionine-rich 2S albumin from sunflower seeds showed four intra-chain disulphide bonds which are homologous with those in a related heterodimeric albumin from lupin seeds (conglutin δ). Similar conserved disulphide bonds are also present in α-gliadin and γ-gliadin storage proteins of wheat, but a lower level of conservation is present in a further related group of proteins, the cereal inhibitors of α-amylase and trypsin. These differences may relate to the different functions of the proteins.

【 授权许可】

Unknown