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

Abstract:

: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.

journal_name

Acta Haematol

journal_title

Acta haematologica

authors

Dassin E,Bourebia J,Najean Y,Rosset AM

doi

10.1159/000206900

subject

Has Abstract

pub_date

1983-01-01 00:00:00

pages

249-53

issue

4

eissn

0001-5792

issn

1421-9662

journal_volume

69

pub_type

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