Open AccessIdentification of a 148‐kDa surface lectin from Giardia lamblia with specificity for α‐methyl‐d‐mannoside
Author(s) -
Sreenivas K.,
Ganguly Nirmal K.,
Ghosh Sujata,
Sehgal Rakesh,
Mahajan Ramesh C.
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07910.x
Subject(s) - lectin , identification (biology) , chemistry , biology , biochemistry , ecology
A lectin specific for α‐methyl‐d‐mannoside was purified from the membrane extract of Giardia lamblia by a combination of gel filtration chromatography on Sephadex G‐75 and Superose 6‐HR 10/30. The homogeneity of the lectin was established by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular mass of the native protein was 148 kDa. The lectin agglutinated rabbit erythrocytes in the presence of Ca 2+ at 37 °C and pH 7.O. The maximum activity of the lectin was obtained after trypsin treatment. The inhibition study clearly suggests that the binding site of the lectin recognizes α‐methyl‐d‐mannoside as the immunodominant sugar.