Preparation and Characterization of Guanidinated Trypsinogen and ∈-Guanidinated Trypsin

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

doi:10.1021/bi00727a009

Preparation and Characterization of Guanidinated Trypsinogen and ∈-Guanidinated Trypsin

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

Biochemistry & Structural Biology

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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 language	English (US)
Pages (from-to)	414-420
Number of pages	7
Journal	Biochemistry
Volume	12
Issue number	3
DOIs	https://doi.org/10.1021/bi00727a009
State	Published - Jan 1 1973

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Biochemistry

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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.",

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year = "1973",

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N2 - 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.

AB - 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.

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Preparation and Characterization of Guanidinated Trypsinogen and ∈-Guanidinated Trypsin

Abstract

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