Isolation and characterization of two antigenic glycoproteins from the pollen of Prosopis juliflora.
Two antigenically active glycoprotein fractions were isolated from crude extract of the pollen of Prosopis juliflora using DEAE-cellulose ion exchange chromatography. The glycoproteins gave single band on polyacrylamide gel electrophoresis. The molecular weight of these two glycoprotein was 20,000 and 10,000 as determined by gel filtration on Sephadex G-75. With the help of crossed immunoelectrophoresis and gel diffusion crude extract exhibited twelve and three precipitating antigens suggesting its heterogeneous nature; and the purified glycoprotein fractions however formed single precipitin band on gel diffusion test and immunoelectrophoresis. As tested by ELISA the polyclonal antisera raised in rabbit showed strong binding affinity with glycoprotein of MW 20,000. These result indicates that the two glycoprotein fractions are not antigenically identical.
Thakur
I S
IS
Department of Environmental Sciences, College of Basic Sciences and Humanities, G.B. Pant University of Agriculture and Technology, Pantnagar, Nainital, India.
D000485:Allergens / Q000737:chemistry / Q000302:isolation & purification*; D000941:Antigens / Q000302:isolation & purification*; D005591:Chemical Fractionation; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000737:chemistry / Q000276:immunology* / Q000302:isolation & purification; D008970:Molecular Weight; D011058:Pollen / Q000032:analysis / Q000276:immunology*
D000485:Allergens; D000941:Antigens; D006023:Glycoproteins