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A T-antigen-binding lectin from Channa leucopunctatus (Murrel) plasma
S R Manihar1, R H Das, H R Das
1C.S.I.R. Centre for Biochemicals, Delhi University Campus, India.
Carbohydrate Research
|June 25, 1991
Summary
Researchers isolated a specific lectin from Channa leucopunctatus fish plasma that targets blood group A. This purified lectin, a glycoprotein, requires divalent cations for its hemagglutinating activity.
Area of Science:
- Biochemistry
- Immunology
- Zoology
Background:
- Channa leucopunctatus fish plasma exhibits non-specific agglutination of human A,B,O blood-group erythrocytes.
- The plasma contains three distinct hemagglutinating activities.
- These activities can be differentiated using specific blood-group erythrocytes.
Purpose of the Study:
- To isolate and characterize the specific blood group A agglutinating activity from Channa leucopunctatus plasma.
- To determine the biochemical properties and requirements of the purified lectin.
Main Methods:
- DEAE-cellulose column chromatography for initial separation.
- Affinity chromatography using 2-acetamido-2-deoxy-D-galactose coupled to epoxy-activated Sepharose 6B for purification.
- Poly(acrylamide) gel electrophoresis, isoelectric focusing, immunodiffusion, and cross-immunoelectrophoresis for homogeneity assessment.
Main Results:
- A homogeneous lectin with blood group A specificity was purified.
- The lectin has a molecular weight of 140,000 Da, composed of two identical subunits.
- Its isoelectric point is 4.6, and it is a glycoprotein requiring divalent cations (Ca2+, Mg2+, or Mn2+) for activity.
- Potent inhibitors include 2-acetamido-2-deoxy-D-galactose and related compounds.
Conclusions:
- The study successfully isolated and characterized a novel lectin from Channa leucopunctatus plasma with specific affinity for blood group A.
- The lectin's properties, including its requirement for divalent cations and specific inhibitory compounds, provide insights into its molecular mechanism.