Abstract
[ 3H]Azidobutyryl clentiazem, a new photoactivatable diltiazem derivative, has a higher binding affinity than azidobutyryl diltiazem. It can be covalently incorporated into the α 1 subunit of the skeletal muscle calcium channel by UV irradiation, which allows the benzothiazepine binding site to be determined. The photolabeled α 1 subunit and its proteolytic fragments were analyzed with a panel of sequence-directed antibodies. The results suggest that the linker region between segment S5 and S6 of domain IV is involved in benzothiazepine binding. This site is different from the dihydropyridine and verapamil binding sites.
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