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Purification and partial characterization of a liver cell proliferation factor called hepatopoietin

✍ Scribed by Michel Goldberg

Publisher: John Wiley and Sons
Year: 1985
Tongue: English
Weight: 588 KB
Volume: 27
Category: Article
ISSN: 0730-2312
DOI: 10.1002/jcb.240270310

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✦ Synopsis

Max-Planck-lnstitut fur Biochemie, Arbeitsgruppe Experimentelle Medizin 0-8033

Martinsrietl, Federal Republic of Germany

The purification and partial characterization of a liver cell proliferation factor called hepatopoietin are described. Hepatopoietin was isolated from remnant livers or blood plasma of partially hepatectomized rats and purified approximately 13,000-fold. The stokes radius was 2.65 0.2 nm and the apparent molecular weight was calculated to be 38,000 5,000 D. Hepatopoietin is a heat-stable glycoprotein and is organ specific but species nonspecific. In vivo it stimulates about three to four times the DNA synthesis as well as the mitotic rate of the liver of normal rats after i.p. injection. Hepatopoietin is inactivated upon incubation with galactosidase or trypsin-chymotrypsin.

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