Characterization of glycyrrhizin-binding protein kinase from the crude membrane fraction of rat liver

Akira Ishikawa, Ryunosuke Kanamaru, Akira Wakui, Shin ichiro Kanno, Kenzo Ohtsuki

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Using GL-affinity column chromatography, a casein phosphorylating protein kinase was purified selectively from the crude membrane fraction of rat liver. The biochemical characteristics of the purified kinase (approximately Mr 210 kDa) are very similar to those reported for polypeptide-dependent protein kinase (kinase P). Moreover, low doses of GL selectively inhibit phosphorylation of Mr 35-36 kDa polypeptides (which are cross-reacted with anti-lipocortins I and II) by the kinase invitro. These results suggest that the anti-inflammatory activity of GL may involve the impairment of the physiological functions of lipocortins through their specific modification by the kinase at the cell membrane level.

Original languageEnglish
Pages (from-to)876-882
Number of pages7
JournalBiochemical and biophysical research communications
Volume167
Issue number3
DOIs
Publication statusPublished - 1990 Mar 30
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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