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Accession number;01A0228953
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| Title;Molecular Recognition and Effect on Chaperone Activity for Heat Shock Protein (HSP) by Fluorescent Cyclodextrin. |
| Author;
NARITA MIYUKI
(Akita Univ., Facutity of Engineering and Resource Sci, JPN)
ITO HIDEAKI
(Akita Univ., Sch. of Med.)
HAMADA FUMIO
(Akita Univ., Facutity of Engineering and Resource Sci, JPN)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.15th;NO.;PAGE.22-23(2000)
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| Figure&Table&Reference;FIG.2, REF.5 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Molecular recognition and effect on chaperone actvity for heat shock protein such as HSP70 and 90 by 6A,6D-bis dansyl-modified .BETA.-cyclodextrin as a host has been studied. The fluorescence intensity of the host was decreased when HSP70 and 90 were added to the host solution. The binding constsnts of the host were using 1:1 complex formation type equation by employing the guest-induced fluorescence variations. The host exhibited higher binding ability for HSP70 than that of HSP90. The effect of the host on chaperone activity for HSP70 and 90 was investigated by measuring absorption of aggregation of C.S. (citrate synthase). The host can regulate C.S. aggregation when HSP70 or 90 was presented. In this system, the fluorescent cyclodextrin can recognize these protein and alter their bio-activity such as molecular chaperone. (author abst.) |
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