Preparation and Characterization of Guanidinated Trypsinogen and ∈-Guanidinated Trypsin

Neal C. Robinson, Hans Neurath, Kenneth A. Walsh

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Reaction of bovine trypsinogen with 1-guanyl-3,5-dimethylpyrazole converted all 15 lysine residues to homoarginyl residues. Trypsin could not activate guanidinated trypsinogen but an acid protease from Aspergillus oryzae generated active ∈-guanidinated trypsin by cleaving the Har6–Ile7 bond in the modified zymogen and releasing the activation peptide Val-(Asp)4-Har. After purification by affinity chromatography, the ∈-guanidinated enzyme contained 0.94–0.98 active site/molecule and exhibited the same specific activity toward benzoyl-L-arginine ethyl ester as β-trypsin.

Original languageEnglish (US)
Pages (from-to)414-420
Number of pages7
JournalBiochemistry
Volume12
Issue number3
DOIs
StatePublished - Jan 1 1973

ASJC Scopus subject areas

  • Biochemistry

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