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Partial purification of a thrombocytopoiesis stimulating factor present in the serum of thrombocytopenic rats.

Successive chromatographic procedures made it possible to isolate thrombocytopoietin from the serum of thrombocytopenic rats. The following steps were taken: DEAE-cellulose phosphate chromatography, Sephadex chromatography, exclusion chromatography on DEAE-Sephadex A-50 gel. The apparent molecular weight of thrombocytopoietin was about 48,000 daltons. Like erythropoietin, thrombocytopoietin is a glycoprotein, its molecular weight is similar. A single form is obtained only when the different purification steps last less than 10 days. Beyond that time, partial degradation may occur.