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Biochim Biophys Acta. 1983 Aug 16;746(3):217-9.
Resonance energy transfer was used to monitor the interaction of an active-site-directed fluorescent inhibitor, N-(5-dimethylaminonaphthalene-1-sulfonyl)-3-aminobenzene boronic acid, and lipoprotein lipase (EC 220.127.116.11). The binding of this probe to the active site of lipoprotein lipase had an association constant, Ka, of 1.1 X 10(6) M-1, indicating a strong interaction. The binding was displaced competitively by benzene boronic acid. The method described provides a sensitive procedure to probe the active site of lipoprotein lipase.