Description

• Specificity: Subtilisin A is a member of the Serine S8 Endoproteinase family. It has broad specificity with a preference for a large uncharged residue in the P1 position. It hydrolyzes native and denatured proteins, and is active under alkaline conditions.
• Application: The enzyme from Sigma has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.[1] It has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral DNA.[2]
• Biochem/physiol Actions: Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .
• Physical properties: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa.
• Unit Definition: One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).
• Analysis Note: Amino acid analysis and isoelectric focusing electrophoresis consistent with subtilisin Carlsberg.