Abstract
A single cysteine residue present in human plasma alpha 1-proteinase inhibitor was labeled with a fluorescent sulfhydryl reagent, N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine. The resulting fluorescent inhibitor retained nearly full inhibitory activity and formed complexes with bovine chymotrypsin, porcine pancreatic elastase, and bovine trypsin as revealed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Association rate constants for the interactions of the labeled inhibitor with the proteinases were determined to be 1.5 (+/- 0.4) X 10(6), 3.3 (+/- 0.3) X 10(5), and 1.4 (+/- 0.3) X 10(5) M-1 X s-1 for chymotrypsin, elastase, and trypsin, respectively. These values were found to be only slightly lower than those of the unlabeled inhibitor. Fluorescence emission spectra of the labeled inhibitor in the absence and presence of each proteinase were also examined, and little difference was observed between them.
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