GTP Hydrolysis by Guinea Pig Liver Transglutaminase

Overview

Journal Biochem Biophys Res Commun

Publisher Elsevier

Specialty Biochemistry

Date 1989 Aug 15

PMID 2569868

Citations 23

Authors

K N Lee

P J Birckbichler

M K Patterson Jr

Affiliations

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Abstract

Homogeneous guinea pig liver transglutaminase was purified from a commercially available enzyme preparation by affinity chromatography on GTP-agarose. The purified transglutaminase exhibited a single band of apparent Mr = 80,000 on sodium dodecyl sulfate polyacrylamide gel and Western blotting and had enzyme activity of both transglutaminase and GTPase. The guinea pig liver transglutaminase has an apparent Km value of 4.4 microM for GTPase activity. GTPase activity was inhibited by guanine nucleotides in order GTP-gamma-S greater than GDP, but not by GMP. These results demonstrate that purified guinea pig liver transglutaminase catalyzes GTP hydrolysis.

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