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L5006

Sigma-Aldrich

Leucine Aminopeptidase, microsomal from porcine kidney

Type IV-S, ammonium sulfate suspension, 10-40 units/mg protein (Bradford)

Synonym(s):

Aminopeptidase M, Aminopeptidase N, Cathepsin III, LAP, Leucinamide aminopeptidase, Leucinaminopeptidase

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About This Item

CAS Number:
9054-63-1
Enzyme Commission number:
3.4.11.2 (BRENDA, IUBMB)
EC Number:
232-942-5
MDL number:
MFCD00131501
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type IV-S

Quality Level

200

form

ammonium sulfate suspension

specific activity

10-40 units/mg protein (Bradford)

storage temp.

2-8°C

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General description

Leucine Aminopeptidase belongs to the family of metalloprotease.

Application

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

Biochem/physiol Actions

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

Unit 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.

Physical form

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

inhibitor

Product No.
Description
Pricing

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity
Grembecka J, et al.
Journal of medicinal chemistry, 46(13), 2641-2655 (2003)
Rossella Galati et al.
Zeitschrift fur Naturforschung. C, Journal of biosciences, 58(7-8), 558-561 (2003-08-27)
The ability of synthetic protein fragments to survive the degradative action of aminopeptidases and serum proteolytic enzymes can be remarkably enhanced by slight modifications at their N-terminal alpha-amino group. This can be achieved by addition of beta-alanine or amino acids
Intestinal digestive resistance of immunodominant gliadin peptides
Hausch F, et al.
American Journal of Physiology: Gastrointestinal and Liver Physiology, 283(4), G996-G1003 (2002)
Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain
Takaki Y, et al.
The Journal of Biological Chemistry, 128(6), 897-902 (2000)
Debittering of a Tryptic Digest of Bovine p-casein Using Porcine Kidney General Aminopeptidase and X-Prolydipeptidyl Aminopeptidase from Lactococcus lactis subsp. cremoris AM2
Barry CM, et al.
Journal of Food Science, 65(7), 1145-1150 (2000)
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