title: Partial characterization of the E rosette restoring factor (RRF) from normal human serum.
abstract: A factor that restores E rosette formation (RRF) was isolated and purified on AMICON membranes. After initial purification, the product showed minimal activity at a concentration of 2 microgram protein per sample. Chromatography on Sephadex G-150 of the partly purified factor caused a further rise in activity to 0.15 microgram per sample. RRF restores normal rosette formation not only by lymphocytes isolated from peripheral blood of patients with active pulmonary tuberculosis, but also stimulated E rosette formation by bone marrow cells. The factor is thermolabile, being completely inactivated at 56 degrees C and partly at 37 degrees C, and is sensitive to freezing and thawing. Its molecular weight is about 10 x 10(3) to 20 x 10(3).
mesh_terms: D001798:Blood Proteins; D002850:Chromatography, Gel; D006801:Humans; D008214:Lymphocytes / Q000276:immunology*; D008970:Molecular Weight; D012397:Rosette Formation; D013951:Thymus Hormones / Q000097:blood; D014397:Tuberculosis, Pulmonary / Q000097:blood
chemical_list: D001798:Blood Proteins; D013951:Thymus Hormones