Enzymes which catalyze the hydrolysis of the chromogenic substrate n-leucyl-/?-naphthylamide have been demonstrated in human serum and tissues.Since increased activity of the serum enzyme or enzymes usually reflects intra-or extrahepatic biliary obstruction, its assay has been reported to be of value in the diagnosis and management of hepatobiliary disease (1).This enzyme, initially termed leucine aminopeptidase, was considered to be similar to that isolated from hog kidney (2).However, recent studies have indicated that the serum enyzme is neither specific for leucymaphthylamides nor identical with the hog kidney enzyme (3, 4).Many tissues contain enzymes (isoenzymes) which hydrolyze n-leucyl+-naphthylamide, but the liver appears to be the principal source of the normal serum component.The isolation and partial purification of this enzyme from human liver was undertaken to study its biochemical properties and to compare it with the serum enzyme.
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Smith et al. (1965) studied this question.