Journal of the American Chemical Society p. 7299 - 7306 (1982)
Update date:2022-08-05
Topics:
Melhado, L. Lee
Peltz, Stuart W.
Leytus, Steven P.
Mangel, Walter F.
Two active-site titrants of serine proteases, fluorescein mono-p-guanidinobenzoate hydrochloride (FMGB*HCl) and fluorescein di-p-guanidinobenzoate dihydrochloride (FDGB*2HCl), have been synthesized, purified, and chemically and enzymatically characterized.Electronic absorbtion and fluorescence emission spectra, fluorescence lifetimes and quantum yields, solubilities, and rates of spontaneous hydrolysis at pH 7-10 are reported.Macroscopic and microscopic kinetic constants for interaction of FMGB*HCl with trypsin, urokinase, plasmin, and trombin have been determined.FMGB*HCl, which rapidly releases fluorescein upon formation of a stable acyl-enzyme intermediate with tripsin and other trypsin-like enzymes, is the most sensitive active-site titrant for serine proteases yet described.
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Doi:10.1248/cpb.30.2586
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