Partial Purification of a Thrombocytopoiesis Stimulating Factor Present in the Serum of Thrombocytopenic Rats
| Autor: | Y. Najean, E. Dassin, A.M. Rosset, J. Bourebia |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Blood Platelets
Chromatography DEAE-Cellulose Selenium chemistry.chemical_compound medicine Animals Platelet Sodium dodecyl sulfate Selenomethionine Thrombopoietin Glycoproteins Radioisotopes chemistry.chemical_classification Sodium Dodecyl Sulfate Rats Inbred Strains Hematology General Medicine Phosphate Thrombocytopenia Hematopoiesis Rats Biochemistry chemistry Sephadex Erythropoietin Electrophoresis Polyacrylamide Gel Glycoprotein medicine.drug |
| Zdroj: | Acta Haematologica. 69:249-253 |
| ISSN: | 1421-9662 0001-5792 |
| DOI: | 10.1159/000206900 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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