TY - JOUR
AU - Rojkind, Marcos
AB - A 220-kilodalton (kDa) protein with lectin properties was isolated from Entamoeba histolytica strain HM1:IMSS and was purified by Sepharose 4B chromatography and electroelution from 5% SDS-polyacrylamide gels. The protein contains 9% carbohydrate by weight; is rich in hydrophobic residues; and is very immunogenic in mice, hamsters, and rabbits. The protein binds to fixed monolayers of MDCK cells and inhibits trophozoite attachment to the cultured cells. The 220-kDa protein agglutinates human erythrocytes, and agglutination is inhibited by micro molar concentrations of hyaluronic acid, chitin, chitinderived products (chitotriose), and antibodies to the purified protein. The 220-kDa protein is recognized by an antibody to the membrane but not by antibodies to other subcellular fractions. We therefore suggest that this 220-kDa protein with lectin properties is a component of the plasma membrane and could be one of the putative “receptor” molecules involved in cell and/or matrix attachment.
TI - Isolation of a 220-Kilodalton Protein With Lectin Properties From a Virulent Strain of Entamoeba histolytica
JF - The Journal of Infectious Diseases
DO - 10.1093/infdis/156.5.790
DA - 1987-11-01
UR - https://www.deepdyve.com/lp/oxford-university-press/isolation-of-a-220-kilodalton-protein-with-lectin-properties-from-a-5u1WBkj0nJ
SP - 790
EP - 797
VL - 156
IS - 5
DP - DeepDyve
ER -