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The lectin nature of α‐galactosidases from Vicia faba seeds
Author(s) -
Dey Prakash M.,
Naik Surbhi,
Pridham John B.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81341-0
Subject(s) - lectin , tetramer , biochemistry , vicia faba , enzyme , mannose , concanavalin a , chemistry , glycoprotein , galactose , biology , botany , in vitro
α‐Galactosidase from Vicia faba seeds has been resolved into three molecular forms, I, II 1 and II 2 , 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.