Purification and characterization of lectin from fruiting body of Ganoderma lucidum -: Lectin from Ganoderma lucidum

被引:42
|
作者
Thakur, Atul
Rana, Monika
Lakhanpal, T. N.
Ahmad, Absar
Khan, M. I. [1 ]
机构
[1] Natl Chem Lab, Div Biochem Sci, Pune 411008, Maharashtra, India
[2] HP Univ, Dept Biosci, Shimla, HP, India
来源
关键词
mushroom; Ganoderma lucidum; purification; thermodynamic properties; glycan binding; ACID-SPECIFIC LECTIN; CHEMICAL MODIFICATION; EDIBLE MUSHROOM; CARBOHYDRATE-BINDING; AGGLUTININ; SPECIFICITY; PROTEINS; FUNGUS; RESIDUES; OLIGOSACCHARIDES;
D O I
10.1016/j.bbagen.2007.05.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A novel 114 kDa hexameric lectin was purified from the fruiting bodies of the mushroom Ganoderma lucidum. Biochemical characterization revealed it to be a glycoprotein having 9.3% neutral sugar and it showed hemagglutinating activity on pronase treated human erythrocytes. The lectin was stable in the pH range of 5-9 and temperature up to 50 degrees C. The hemagglutinating activity was inhibited by glycoproteins that possessed N-as well as O-linked glycans. Chemical modification of the G. lucidum lectin revealed contribution of tryptophan and lysine to binding activity. The thermodynamics of binding of bi- and triantennary N-glycans to G. lucidum lectin was studied by spectrofluorimetry. The lectin showed very high affinity for asialo N-linked triantenary glycan and a preference for asialo glycans over sialylated glycans. The binding was accompanied with a large negative change in enthalpy as well as entropy, indicating primarily involvement of polar hydrogen, van der Waals and hydrophobic interactions in the binding. (C) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:1404 / 1412
页数:9
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