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Small Heat Shock Protein Hsp27 Directly Binds to Alpha/Beta Tnbulin Heterodimer and Inhibits DMSO-Induced Tubulin Polymerization
- Source :
- Biomedical Research. 24:27-30
- Publication Year :
- 2003
- Publisher :
- Biomedical Research Press, 2003.
-
Abstract
- In this study, the interaction between the small heat shock protein Hsp27 and α/β tubulin heterodimer was investigated. First, immunoprecipitation analysis using recombinant Hsp27 and purified tubulin indicated that Hsp27binds with α/β tubulin heterodimer. Next, the effect of Hsp27 on tubulin polymerization was examined. Hsp27 showed the inhibitory effect on dimethylsulfoxide (DMSO)-induced tubulin polymerization. The inhibitory effect was dose-dependent: about 30% inhibition of polymerization was found after addition of 0.85 mg/mL of Hsp27, 70% inhibition was found by 3.4 mg/mL of Hsp27.
- Subjects :
- endocrine system
animal structures
biology
Immunoprecipitation
Alpha (ethology)
macromolecular substances
General Medicine
urologic and male genital diseases
Molecular biology
General Biochemistry, Genetics and Molecular Biology
law.invention
Tubulin
Hsp27
Polymerization
law
Heat shock protein
embryonic structures
biology.protein
Recombinant DNA
Beta (finance)
Subjects
Details
- ISSN :
- 1880313X and 03886107
- Volume :
- 24
- Database :
- OpenAIRE
- Journal :
- Biomedical Research
- Accession number :
- edsair.doi...........8f98c2a0a32ad4e997c23f35cba6293d