Atherosclerosis: the role of lipids.
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Biomedical subjects
Publications and source records attributed to J Loeb.
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The defective autologous MLR was studied in Sjögren's syndrome (SS) in relation to Ia+ cells as determined by reactivity with a monoclonal anti-human Ia antibody. By indirect immunofluorescence, the percentage of Ia+ T lymphocytes was increased in nine of 15 patients. There was no correlation with clinical features or drugs. The percentage of Ia+ T cells in the non-T cell preparations was normal. An inverse correlation was found between the percentage of Ia+ T cells and the proliferative response to autologous non-T cells. Removal of Ia+ T cells enhanced both the autologous MLR and the allogeneic MLR. Thus Ia+ T cells contain suppressor cells in the MLR, but this may not be the sole explanation for the defective autologous MLR.
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Protein kinase activities copurifying with the 72000-Mr DNA-binding protein of adenovirus on DNA-cellulose chromatography and gel filtration in acrylamide/agarose have been partially characterized and purified. One of these kinases was found to phosphorylate efficiently the viral DNA-binding protein in vitro and to be stimulated severalfold by the addition of histones, protamine, or polyamines. The kinase does not, however, phosphorylate histones, protamine, casein, or phosvitin. A second protein kinase was also recovered from single-stranded DNA-cellulose which is able to phosphorylate the 72000-Mr DNA-binding protein, but which is inhibited by the addition of histones. Phosphorylation in vitro of the 72000-Mr DNA-binding protein from the ts125 mutants of adenovirus by the histone-stimulated protein kinase was found to be thermosensitive.
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