Purification and characterization of lectin from fruiting body of Ganoderma lucidum: lectin from Ganoderma lucidum.
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 triantennary 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.
Thakur
Atul
A
Division of Biochemical Sciences, National Chemical Laboratory, Pune-411008, India.
Rana
Monika
M
Lakhanpal
T N
TN
Ahmad
Absar
A
Khan
M I
MI
D006385:Hemagglutination Inhibition Tests; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification*; D011134:Polysaccharides / Q000737:chemistry; D020940:Reishi / Q000737:chemistry*; D013816:Thermodynamics
D037102:Lectins; D011134:Polysaccharides