Leucine Aminopeptidase, microsomal from porcine kidney CAS:9054-63-1

Grade：BR

Vitality：15～25 units/mg protein (biuret)

Vitality definition：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

Physicochemical properties: powder. It is one of the components of urinary enzymes. It is an intracellular lysosomal hydrolase, which is widely distributed in kidney, liver, connective tissue, salivary gland, lymph node and other tissues. The molecular weight is about 255000

Purpose: biochemical research. One of the aminopeptidases in protein hydrolases. These enzymes can cut the amino acids one by one from the outside to the inside from the free amino terminal (N-terminal) of the polypeptide chain. Leucine aminopeptidase has this name not because it can only hydrolyze the peptide bond with leucine (Leu) as the N-terminal residue, but because it hydrolyzes the peptide bond with leucine as the N-terminal at the fastest speed. In fact, it can also act on other amino acids at the N-terminal. Mg2 + or Mn2 + is necessary for the catalytic action of the enzyme. In the early days, it was often used to determine the amino acid sequence of peptides.