title: The characteristics of purified HL60 tuftsin receptors.
abstract: The purification and characteristics of purified HL60 tuftsin receptors are described. Purification was accomplished by affinity chromatography similar to that described earlier, wherein a tuftsin analog Thr-Lys-Pro-Pro-Arg, is covalently linked at the N alpha group to a solid support. The receptor consists presumably of two subunits approximately 66 KDa and 57 KDa. The dissociation constant of the receptor complex is 4.7 X 10(-8) M with 5 X 10(4) receptors per cell. It can form oligomers with an Mr of about 560 KDa suggesting an octomeric structure, assuming the same number of each subunit is associated.
authors.affiliation: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
authors.forename: N J
authors.initials: NJ
authors.lastname: Bump
authors.forename: V A
authors.initials: VA
authors.lastname: Najjar
authors.forename: J
authors.initials: J
authors.lastname: Reichler
mesh_terms: D011232:Chemical Precipitation; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D015473:Leukemia, Promyelocytic, Acute; D011971:Receptors, Immunologic / Q000032:analysis / Q000648:ultrastructure; D014405:Tuftsin / Q000031:analogs & derivatives / Q000096:biosynthesis; D014407:Tumor Cells, Cultured
chemical_list: D011971:Receptors, Immunologic; C029695:tuftsin receptor; D014405:Tuftsin