TAILIEUCHUNG - Báo cáo Y học: Characterization of the 105-kDa molecular chaperone Identification, biochemical properties, and localization

We have characterized the biochemical properties of the testis and brain-specific 105-kDa protein which is cross-reacted with an anti-bovine HSP90 antibody. The protein was induced ingermcells byheat stress, resulting inaprotein which is one of the heat shock proteins [Kumagai, J., Fuk-uda, J., Kodama, H., Murata, M., Kawamura, K., Itoh, H. &Tanaka,T. (2000)Eur. , 3073–3078]. In the present study,we characterized thebiochemical propertiesof the protein. | Eur. J. Biochem. 1-10 2002 FEBS 2002 doi Characterization of the 105-kDa molecular chaperone Identification biochemical properties and localization Mika Matsumori1 2. Hideaki Itoh1. Itaru Tovoshima3. Atsushi Komatsuda4. Ken-ichi Sawada4 Jun Fukuda5 Toshinobu Tanaka5 Atsuva Okubo6. Hirovuki Kinouchi6. Kazuo Mizoi6. Tokiko Hama7. Akira Suzuki1 B Bf FB B B B B B Bf BB W B BB B B BB B w BB B B V B B w w BB Bf B B B B B w B B Bl B Bl B B B w B B B B wBB F B Bf B B B B Bb B B B B w B B w B B B BB B B B BB B Bl w B B BB B F w F w B w B Fumio Hamada8 Michiro Otaka3 Yutaka Shoji2 and Goro Takada2 1 Department of Biochemistry 2Department of Pediatrics 3First Department of Internal Medicine iThird Department of Internal Medicine 5Department of Gynecology and 6Department of Neurosurgery Akita University School of Medicine Akita City Japan President s Frontier Laboratory. Mitsubishi Kasei Institute of Life Sciences Tokyo Japan 8Department of Material-Process Engineering and Applied Chemistry for Environment Akita University Faculty of Engineering and Resource Science Akita City Japan We have characterized the biochemical properties of the testis and brain-specific 105-kDa protein which is crossreacted with an anti-bovine HSP90 antibody. The protein was induced in germ cells by heat stress resulting in a protein which is one of the heat shock proteins Kumagai J. Fukuda J. Kodama H. Murata M. Kawamura K. Itoh H. Tanaka T. 2000 Eur. J. Biochem. 267 3073-3078 . In the present study we characterized the biochemical properties of the protein. The 105-kDa protein inhibited the aggregation of citrate synthase as a molecular chaperone in vitro. ATP MgCl2 has a slight influence of the suppression of the citrate synthase aggregation by the 105-kDa protein. The protein possessed chaperone activity. The protein was able to bind to ATP-Sepharose like the other molecular chaperone HSP70. A partial amino-acid sequence 24 amino-acid residues of the protein was .

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