Leucine Aminopeptidase, microsomal from porcine kidney

Leucine Aminopeptidase belongs to the family of metalloprotease.

Leucine Aminopeptidase, microsomal from porcine kidney has been used in the isolation of neprilysin (NEP) from rodent brain-C5 and for peptide digestion.

Leucine Aminopeptidase possesses broad substrate-specificity. It hydrolyzes peptides up to the proline residue and does not continue to degrade beyond proline.

Suspension in 3.5 M (NH₄)₂SO₄ solution, pH 7.7, containing 10 mM MgCl₂

One unit will hydrolyze 1.0 μmole of L-leucine-p-nitroanilide to L-leucine and p-nitroaniline per min at pH 7.2 at 37 °C. (At 25 °C, approx. 40% of the activity at 37 °C is obtained.) The activity obtained using L-leucine p-nitroanilide as substrate is 2-5 times that obtained with L-leucinamide as substrate.