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Purification and subunit structure of hepatocyte growth factor from rat platelets.

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Affiliations

  • 1. Institute for Enzyme Research, University of Tokushima, Japan.
      Authors
    • Nakamura T 1
    (1 author)

FEBS Letters, 01 Nov 1987, 224(2):311-316
https://doi.org/10.1016/0014-5793(87)80475-1 PMID: 3319692 

Abstract 

A hepatocyte growth factor (HGF) that stimulates DNA synthesis of adult rat hepatocytes in primary culture was purified as a homogeneous material from platelets of 1000 rats by a four-step procedure: stimulation of its release from platelets by thrombin, cation-exchanger fast protein liquid chromatography (FPLC) on a Mono S column, heparin-Sepharose CL-6B chromatography, and reverse-phase HPLC on a C4 column. The purified HGF stimulated DNA synthesis of adult rat hepatocytes in primary culture at 1 ng/ml and was maximally effective at 5 ng/ml, being about twice as potent as EGF at this concentration. HGF did not stimulate DNA synthesis of Swiss 3T3 cells. It was found to be a heat- and acid-labile protein that was inactivated by reduction with dithiothreitol. The purified HGF had a molecular mass of 82 kDa, as estimated by SDS-PAGE, and was found to be a heterodimer which dissociated into a large subunit of 69 kDa and a small one of 34 kDa by SDS-PAGE under reducing conditions. These biological and chemical properties showed that HGF was not identical with any known growth factors, including platelet-derived growth factor (PDGF).

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Read article at publisher's site: https://doi.org/10.1016/0014-5793(87)80475-1

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