Abstract
Summary The aminopeptidases from Euglena gracilis Klebs, strain Z, were investigated by polyacrylamide gel electrophoresis and affinity chromatography. Nine multiple moleculare forms (AP) from (Leucine)-aminopeptidase (AP6) were characterized by disc electrophoresis. They differ in molecular weight and in specificity against aminoacid naphthylamides. A disaggregation of (Leucine)-aminopeptidase (AP6) into active subunits API and APII by EDTA can be demonstrated.
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