Automated assay for α1-antitrypsin with N-α-benzoyl-DL-arginine-p-nitroanilide as trypsin substrate and standardized with p-nitrophenyl-p'-guanidinobenzoate as titrant for trypsin active sites

J. H. Eckfeldt, R. T. Light, C. Leiendecker-Foster

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Abstract

α1-Antitrypsin is the most abundant of several serum protease inhibitors. Its deficiency is associated with an increased incidence of emphysema in adults, jaundice in newborns, and childhood cirrhosis. The authors describe an automated functional assay for the Instrumentation Laboratory's Multistat III Microcentrifugal Analyzer with N-α-benzoyl-DL-arginine-p-nitroanilide as trypsin substrate. The assay is standardized in terms of moles of trypsin active sites inhibited per liter of serum, by use of a chromogenic titrant for trypsin active sites, p-nitrophenyl-p'-guanidinobenzoate. The method is rapid, precise, and independent of trypsin supplier, and results correlate well with those by a manual chromogenic and a nephelometric assay.

Original languageEnglish (US)
Pages (from-to)1108-1112
Number of pages5
JournalClinical chemistry
Volume28
Issue number5
StatePublished - Jan 1 1982

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