Concomitant Preparative Isolation of Calmodulin and Heat Shock Protein (hsp90) from Bovine Testes

We have described a convenient procedure for isolating large amounts of both calmodulin and the 90-kDa heat shock protein (hsp90) from bovine testes. These two proteins coeluted from phenyl-Sepharose during calcium-dependent hydrophobic interaction chromatography. The hsp90 was separated from calmod...

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Bibliographic Details
Published inProtein expression and purification Vol. 4; no. 5; pp. 417 - 424
Main Authors Wright, L.S., Finn, K.A., Siegel, F.L.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.10.1993
Subjects
Amino Acid Sequence
Animals
Calmodulin - isolation & purification
Cattle
Chemical Precipitation
Chromatography, Affinity
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Heat-Shock Proteins - isolation & purification
Male
Molecular Sequence Data
Testis - chemistry
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Summary:We have described a convenient procedure for isolating large amounts of both calmodulin and the 90-kDa heat shock protein (hsp90) from bovine testes. These two proteins coeluted from phenyl-Sepharose during calcium-dependent hydrophobic interaction chromatography. The hsp90 was separated from calmodulin by gel filtration, purified by reverse-phase HPLC or lectin affinity chromatography, and identified by N-terminal amino acid sequence and immunoblotting with hsp90-specific monoclonal antibody. The N-terminus of bovine hsp90 shared 93% amino acid identity with the murine α-isoform of hsp90. A third major testes protein of 97 kDa was also isolated with this protocol and was found to be homologous to the 94-kDa glucose-regulated protein.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:1046-5928
1096-0279
DOI:10.1006/prep.1993.1055