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 antiHsp90 antibodies. The Chromatographie 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 language||English (US)|
|Number of pages||8|
|State||Published - Dec 1 1998|
- Heat shock protein
- Troponin components
ASJC Scopus subject areas