Open AccessThe N-acetylgalactosamine and lactosamine specific lectin from Iris hybrida leaves.
Author(s) -
Mirosława Ferens-Sieczkowska,
Magdalena Orczyk-Pawiłowicz,
Bronisława Morawiecka
Publication year - 1997
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1997_4425
Subject(s) - lectin , chemistry , galactose , sugar , biochemistry , concanavalin a , glycoprotein , in vitro
The lectin isolated from the leaves of Iris hybrida binds specifically N-acetyl-galactosamine and lactose. Its molecule consists of two identical subunits bound by disulfide bonds. The lectin is a glycoprotein containing about 12% of sugars. It binds asialoglycoproteins containing complex type sugar chains. The binding is reduced by half at the concentration of 0.15 to 0.40 mM of the galactose containing disaccharides irrespectively to a type of galactose isomer. This indicates rather broad specificity of I. hybrida leaf lectin.