[CITATION][C] The oxidative inactivation of human alpha-1-proteinase inhibitor. Further evidence for methionine at the reactive center.
D Johnson, J Travis - Journal of Biological Chemistry, 1979 - Elsevier
D Johnson, J Travis
Journal of Biological Chemistry, 1979•ElsevierMethods Inhibition Assays-Assays for inhibitory activity were performed by measuring the
decrease in enzymatic activity caused by preincubation with either native or oxidized (YI-PI
(2). The inhibitory activity of unmodified inhibitor was always taken as 100%. Porcine
elastase activity was measured by the procedure of Bieth et al.(9) using Suc-(Ala) sp-
nitroanilide as substrate. Trypsin activity was monitored by the method of Schwert and
Takenaka(10) using Bz-L-Arg-OEt, while chymotrypsin was assayed with Bz-L-Tyr-OEt by …
decrease in enzymatic activity caused by preincubation with either native or oxidized (YI-PI
(2). The inhibitory activity of unmodified inhibitor was always taken as 100%. Porcine
elastase activity was measured by the procedure of Bieth et al.(9) using Suc-(Ala) sp-
nitroanilide as substrate. Trypsin activity was monitored by the method of Schwert and
Takenaka(10) using Bz-L-Arg-OEt, while chymotrypsin was assayed with Bz-L-Tyr-OEt by …
Methods
Inhibition Assays-Assays for inhibitory activity were performed by measuring the decrease in enzymatic activity caused by preincubation with either native or oxidized (YI-PI (2). The inhibitory activity of unmodified inhibitor was always taken as 100%. Porcine elastase activity was measured by the procedure of Bieth et al.(9) using Suc-(Ala) sp-nitroanilide as substrate. Trypsin activity was monitored by the method of Schwert and Takenaka(10) using Bz-L-Arg-OEt, while chymotrypsin was assayed with Bz-L-Tyr-OEt by the method of Kang
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