The diagnostic value of serum leucine aminopeptidase

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The Diagnostic Value of Serum Leucine Aminopeptidase.

Serum leucine aminopeptidase determination was found to be a useful screening procedure for hepatobiliary disease in jaundiced and unjaundiced patients. Values under 1,000 units are of no help in the differential diagnosis of jaundice but values above 1,000 units are highly indicative of biliary obstruction. The differentiation of intra- from extrahepatic obstruction as well as of malignant fro...

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The specificity of leucine aminopeptidase.

Since Linderstr@m-Lang’s demonstration that the hydrolysis of Lleucylglycine (LG) is due to a distinctileucyl peptidase (l), various studies have shown that this enzyme is widely distributed (24) and requires for its activity the presence of Mn++ or Mg++ ions (2, 5). The enzyme has been regarded as a typical aminopeptidase (5), since it does not hydrolyze acylated compounds Such as benzoyl-L-le...

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Leucine Aminopeptidase (Bovine Lens)

The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,...

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Leucine Aminopeptidase (Bovine Lens)

Spark emission and atomic absorption spectroscopy of crystalline leucine aminopeptidase (bovine lens) (EC 3.4.1.1) shows the presence of 2 zinc atoms per subunit molecular weight of 54,000 (12 zinc atoms per oligomer of 320,000). Removal of zinc by dialysis yields a zinc-free product with no enzymatic activity which upon readdition of Zn2+, regains full activity with the concomitant binding of ...

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Leucine Aminopeptidase (Bovine Lens)

The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,...

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ژورنال

عنوان ژورنال: Journal of Clinical Pathology

سال: 1964

ISSN: 0021-9746

DOI: 10.1136/jcp.17.1.52