E0885

Enterokinase from porcine intestine

lyophilized powder, ≥100 units/mg protein

• Synonyme(s) : Enteropeptidase
• CAS Number: 9014-74-8
• Numéro CE : 3.4.21.9 (BRENDA, IUBMB)
• Numéro CE : 232-761-1
• Numéro MDL: MFCD00131020
• Code UNSPSC : 12352204
• eCl@ss : 32160410
• Nomenclature NACRES : NA.54

Propriétés

• Forme: lyophilized powder
• Niveau de qualité: 200
• Activité spécifique: ≥100 units/mg protein
• Poids mol.: 150 kDa
• Produit purifié par: chromatography
• Composition: Protein, ≥20% Lowry
• Activité étrangère: aminopeptidase ≤1.5%; trypsin ≤1%, free
• Température de stockage: −20°C

Description

Application

Enterokinase from porcine intestine has been used in a study to investigate complementary DNA cloning and sequencing of rat enteropeptidase. Enterokinase from porcine intestine has also been used to learn more about the insulinotropic region of the gastric inhibitory polypeptide.

The enzyme from Sigma has been used to activate zymogens in order to detect trypsin activity. The study to investigated the structural and evolutionary consequences of unpaired cysteines in trypsinogen. The product has been used to measure trypsin while studying the effect of pesticide induced alterations in gene expression in the lobster, Homarus americanus The enzyme from Sigma has been used to develop a novel assay for measuring levels of lipid-free apoA-I in the presence of lipid-bound apoA-I. Enteropeptidase can specifically cleave human lipid-free apoA-I but not its lipid-bound form resulting in an N-terminal fragment of 22 kDa. It has also been used in a study to examine the effect of calcium and phytic acid on the activation of trypsinogen and the stability of trypsin.

Actions biochimiques/physiologiques

Enterokinase is a membrane bound serine protease that specifically and rapidly converts trypsinogen to trypsin, thereby, triggering the conversion of other zymogens to active enzymes. It has a molecular mass of approximately 150 kDa. The enzyme is a heterodimer consisting of 35-47 kDa subunits. The light and the heavy chains are linked by two disulfide bridges. It is a glycoprotein containing 35% carbohydrate. The polypeptide chain of trypsinogen is hydrolyzed only after an -(Asp)₄-Lys- sequence. The enzyme is inhibited by soybean trypsin inhibitor. Enterokinase is typically used in protein modification and amino acid sequence determination.

Définition de l'unité

One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25 °C.

Forme physique

Lyophilized powder containing sodium phosphate buffer salts

Informations sur la sécurité

• Code de la classe de stockage: 11 - Combustible Solids
• Classe de danger pour l'eau (WGK): WGK 3
• Point d'éclair (°F): Not applicable
• Point d'éclair (°C): Not applicable
• Équipement de protection individuelle: Eyeshields, Gloves, type N95 (US)