Use of photoaffinity labeling and site-directed mutagenesis for identification of the key residue responsible for extraordinarily high affinity binding of UCN-01 in human alpha1-acid glycoprotein.

doi:10.1074/jbc.M411076200

Article

Use of photoaffinity labeling and site-directed mutagenesis for identification of the key residue responsible for extraordinarily high affinity binding of UCN-01 in human alpha1-acid glycoprotein.

The Journal of biological chemistry - 14 Jan 2005

Katsuki Masaaki, Chuang Victor Tuan Giam, Nishi Koji, Kawahara Kohichi, Nakayama Hitoshi, Yamaotsu Noriyuki, Hirono Shuichi, Otagiri Masaki

Abstract excerpt

7-Hydroxystaurosporine (UCN-01) is a protein kinase inhibitor anticancer drug currently undergoing a phase II clinical trial. The low distribution volumes and systemic clearance of UCN-01 in human patients have been found to be caused in part by its extraordinarily high affinity binding to human alpha1-acid glycoprotein (hAGP). In the present study, we photolabeled hAGP with [3H]UCN-01 without further chemical...

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Use of photoaffinity labeling and site-directed mutagenesis for identification of the key residue responsible for extraordinarily high affinity binding of UCN-01 in human alpha1-acid glycoprotein.

Abstract excerpt

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