Yan Jing Dong

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The interaction of 125I-asialoerythropoietin (asialoepo) with receptors has been characterized both by binding assay and affinity cross-linking. Purified spleen cells from mice infected with the anemia strain of Friend virus (FVA cells) have receptors for 125I-asialoepo with two classes of affinity constant: one with Kd = 0.02-0.03 nM and 300-400 per cell,(More)
Databases’ capability is limited in terms of inference. Especially, when users explore information beyond the scope of data within databases, the databases normally cannot provide the information. The underlying reason of the problem is that queries are answered based on a direct match between a query and data (up to aggregations of the data). We observe(More)
Evidence for an accessory component that can modify the affinity of the erythropoietin (Epo) receptor is presented. Dihydrofolate reductase (DHFR)-deficient Chinese hamster ovary (CHO) cells were transfected with a plasmid containing the Epo receptor cDNA (derived from murine erythroleukemia cells with only low affinity receptors) and DHFR cDNA. The cells(More)
The murine erythroleukemic cell line, IW201, normally expresses only low-affinity erythropoietin receptors. Exposure of these cells for 48 hours to sodium butyrate results in a change in receptor kd from about 600 pmol/L to 100 to 200 pmol/L. This change in affinity is accompanied by downregulation of both receptor number and receptor mRNA. Cells exposed to(More)
The murine erythroleukemic cell lines NN10 and IW32 secrete erythropoietin (Epo) constitutively. Although both cell lines have Epo receptors (Epo-R), they do not respond to external Epo to undergo erythroid differentiation. In both cell lines, hemoglobin synthesis can be induced by hemin or butyrate. We report here on the effects of these two inducers on(More)
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