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Updated: Aug 19, 2026

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Activity and polymorphism of the cobalt-activated acylase in tissues of rodents during development
Abstract:
The activity of cobalt-activated acylase, measured towards N-chloroacetyl- and N-butyryl-gamma-L-glutamyl-beta-naphthylamide, was found in all tissues of the adult animals. In the kidney, liver and small intestine of adult guinea-pig and rat two fractions differing in electrophoretic mobility (fractions 1 and 2) were present. The early foetus contained fraction 2, sometimes accompanied by fraction 3 which later disappeared; on further development of the foetus, fraction 1 appeared. Fraction 1 was distinctly activated by cobalt ions; fractions 2 and 3 were strongly inhibited by deaminated leucylphenylalanine. In the guinea-pig, the molecular weight of the three fractions ranged from 43000 to 59000.
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