Isolation of rabbit liver heat shock protein with molecular weight 90 kD (Hsp90) and its interaction with troponin components and calponin

Y. Sh Ma, N. V. Bogatcheva, N. B. Gusev

Research output: Contribution to journalArticle

Abstract

Using a modified method consisting of chromatography on phenyl-Sepharose, Q-Sepharose, and hydroxyapatite, we isolated a highly purified heat shock protein with molecular weight 90 kD (Hsp90) from rabbit liver. The isolated protein was recognized on immunoblot by commercially available monoclonal anti-Hsp90 antibodies. The chromatographic properties, interaction with actin and calmodulin, phosphorylation in the presence of Mg-ATP, and one-dimensional peptide maps of rabbit liver Hsp90 are similar to the corresponding properties of Hsp90 isolated from other sources. In the presence of soluble carbodiimide and N-hydroxysuccinimide, rabbit liver Hsp90 can be cross-linked with calmodulin, troponin C, troponin I, and calponin. The data obtained indicate that Hsp90 may participate in the assembly of regulatory proteins of the actin filament.

Original languageEnglish (US)
Pages (from-to)1509-1517
Number of pages9
JournalNaihuo Cailiao/Refractories
Volume32
Issue number6
StatePublished - Jan 1 1998
Externally publishedYes

ASJC Scopus subject areas

  • Ceramics and Composites
  • Condensed Matter Physics
  • Metals and Alloys
  • Materials Chemistry

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