Nucleophilic cleavage of the complex between human alpha-1-antitrypsin and porcine pancreatic elastase |
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Authors: | Allen B. Cohen Harold L. James Dagmar Geczy |
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Affiliation: | 1. Department of Medicine, Temple University Health Sciences Center, Philadelphia, Pennsylvania 19140 USA;2. Department of Physiology, Temple University Health Sciences Center, Philadelphia, Pennsylvania 19140 USA |
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Abstract: | Several nucleophilic amines were examined to determine their ability to split the alpha-1-antitrypsin-elastase complex. Hydrazine and hydroxylamine, their methyl derivatives, and methylamine were tested in the pH range of 8 to 10.6. Only hydrazine and methylamine produced complete and clean cleavage of the complex into its inhibitor and enzyme components. When [14C]-methylamine at pH 10.6 was used about 0.3 mol of the nucleophile was specifically bound per mol of the inhibitor component. An interfering reaction between methylamine and the native inhibitor was controlled by preincubation with unlabeled methylamine. |
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Keywords: | Ac-tri-Ala-Me N-acetyl-L-alanyl-L-alanyl-alanine methyl ester DFP diisopropyl fluorophosphate DIP diisopropyl phosphoryl group SDS sodium dodecyl sulfate SDS-PAGE polyacrylamide gel electropherograms in SDS |
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