The lectin nature of α‐galactosidases from Vicia faba seeds

FEBS Letters

Pridham, John B.¹  Naik, Surbhi¹  Dey, Prakash M.¹ 

[1] Department of Biochemistry, Royal Holloway College, Egham Hill, Egham, Surrey, TW20 0EX, England

关键词: Vicia faba;    α-Galactosidase;    Lectin;    Multimolecular form;   

DOI  :  10.1016/0014-5793(82)81341-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-Galactosidase from Vicia faba seeds has been resolved into three molecular forms, I, II¹ and II², respectively. Enzyme I is a tetramer (M _r 160 000) consisting of identical sub-units (M _r 44000 ± 2000). All three forms display lectin activity with glucose/mannose specificity. Enzyme I has been further studied with respect to its lectin specificity and various factors affecting this property. The results indicate that the catalytic and the lectin sites reside in the same protein molecule. The results presented are unique in that the enzyme activity is specific for galactose and its lectin activity is specific for glucose/mannose.

【 授权许可】

Unknown