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The characteristics of purified HL60 tuftsin receptors.
Bump, N J; Najjar, V A; Reichler, J.
Afiliación
  • Bump NJ; Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
Mol Cell Biochem ; 92(1): 77-84, 1990 Jan 18.
Article en En | MEDLINE | ID: mdl-2308578
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.
Asunto(s)
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Bases de datos: MEDLINE Asunto principal: Tuftsina / Receptores Inmunológicos Límite: Humans Idioma: En Revista: Mol Cell Biochem Año: 1990 Tipo del documento: Article
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Bases de datos: MEDLINE Asunto principal: Tuftsina / Receptores Inmunológicos Límite: Humans Idioma: En Revista: Mol Cell Biochem Año: 1990 Tipo del documento: Article