Protéinase K from Tritirachium album

Proteinase K is a stable serine protease with broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents. Proteinase K was isolated from a fungus able to grow on keratin and the enzyme can digest native keratin (hair), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity.

Utile pour l′inactivation protéolytique des nucléases lors de l′isolement de l′ADN et de l′ARN.

Utile pour l′inactivation protéolytique des nucléases lors de l′isolement de l′ADN et de l′ARN.
Élimine les endotoxines qui se lient aux protéines cationiques telles que le lysozyme et la ribonucléase A.
S′est avéré utile pour l′isolement des mitochondries hépatiques, de levure et de haricot mungo.
Détermination de la localisation des enzymes sur les membranes.
Traitement des coupes de tissus incluses en paraffine pour exposer les sites de liaison à l′antigène pour le marquage par anticorps.
Digestion des protéines des échantillons de tissu cérébral pour la recherche sur les prions responsables des encéphalopathies spongiformes transmissibles (EST).

La protéinase K est une sérine protéase très stable et hautement réactive. Des études de cristallographie et de structure moléculaires ont indiqué que cette enzyme appartient à la famille des subtilisines, présentant une triade catalytique au site actif (Asp³⁹-His⁶⁹-Ser²²⁴). Elle est stable dans un vaste éventail d′environnements : pH, sels de tampon, détergents (SDS) et température. En présence de 0,1 à 0,5 % de SDS, la protéinase K reste active et peut digérer diverses protéines et nucléases dans les préparations d′ADN, sans compromettre l′intégrité de l′ADN isolé.

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One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

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