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Abstract
Specific modification of bovine eye lens leucine aminopeptidase by the substrate-like and radioactive tagged diazonium peptide inhibitor, L-(2,3-3H)Phe(pN2+)-L-Phe, was investigated using the technic of affinity and differential labelling. The degree of labelling and the loss of activity increased with excess of the label. A competitive inhibitor diminished the degree of azo-coupling and also the degree of inactivation. First results of tryptic digestion of labelled LAP are given.
Published Version
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