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Abstract
In the present paper we report findings showing the suitability of recrystallized bovine‐lens leucine aminopeptidase as a tool for peptide chemistry.The enzyme is homogeneous with respect to hydrodynamic, chromatographic and electrophoretic separation criteria. It is not contaminated by endopeptidases.The insulin B‐chain (S‐sulfonate) served as model substrate for sequence studies. The initial progress curves of the liberation of the first six amino acids resulted in a sequence expected from the known primary structure. The complete resistance of imido bonds towards the action of leucine aminopeptidase has been proved.Many commercially available protein preparations are found to be contaminated by endopeptidases. We developed an endopeptidase‐detection method in which the leucine aminopeptidase serves as a sensitivity amplifier.
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