P6675
Prolidase from porcine kidney
lyophilized powder, ≥100 units/mg protein
Synonyme(s) :
Aminoacyl-L-proline hydrolase, Imido Dipeptidase, Prolidase, Proline dipeptidase
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About This Item
Produits recommandés
Forme
lyophilized powder
Niveau de qualité
Activité spécifique
≥100 units/mg protein
Composition
Protein, 20-74% Lowry
Température de stockage
−20°C
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Catégories apparentées
Description générale
Prolidase is a cytosolic exopeptidase. It is a homodimeric enzyme which requires divalent cations like manganese as a cofactor in its active site for its function.
Application
Prolidase from porcine kidney has been used:
- in the enzymatic hydrolysis of porcine milk for the recovery of L-glutamine from proteins and peptides
- in the proteolysis of skim milk for the determination of ε-(γ-glutamyl)lysine and free aminoacids
- to determine its effect on the activity of enterococcin A 2000
Prolidase has an important role in recycling of proline and collagen production. It is used to study mutations in the PEPD gene that cause prolidase deficiency. It is used to hydrolyze proteins with C-terminal proline or hydroxyproline residues. Prolidase, product P6675 from porcine kidney, has been used to hydrolyze peptide bonds from the amino terminus when studying enzymatic methylation of membrane proteins.
Actions biochimiques/physiologiques
Prolidase is an enzyme that catalyzes the hydrolysis of the imide bond between an α-carboxyl group and proline or hydroxyproline. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues.
Rare mutation in prolidase gene causes deficiency leading to massive imidodipeptiduria, elevated proline-containing dipeptides in plasma, recurrent infections, mental retardation and skin lesions.
Définition de l'unité
One unit will hydrolyze 1.0 μmole of Gly-Pro per min at pH 8.0 at 40 °C.
Forme physique
Supplied as a lyophilized powder containing Tris buffer salt and MnCl2.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organes cibles
Respiratory system
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
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Les clients ont également consulté
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Haynes TE, et al.
Amino Acids, 37(1), 131-142 (2009)
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We found no data in the literature related to oxidative stress index (OSI), total oxidative status (TOS) and prolidase activity in patients with diabetic neuropathy (DN). In this study, we aimed to evaluate the oxidative status of DN patients via
Prolidase
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Casey M Theriot et al.
Archaea (Vancouver, B.C.), 2011, 565127-565127 (2011-12-14)
Prolidases hydrolyze Xaa-Pro dipeptides and can also cleave the P-F and P-O bonds found in organophosphorus (OP) compounds, including the nerve agents soman and sarin. Ph1prol (PH0974) has previously been isolated and characterized from Pyrococcus horikoshii and was shown to
I M Ota et al.
The Journal of biological chemistry, 264(22), 12879-12884 (1989-08-05)
A group of 23-29-kDa polypeptides in the membranes of bovine rod outer segments are substrates for S-adenosylmethionine-dependent methylation reactions. The bulk of the methyl group incorporation is in base-labile ester-like linkages, and does not appear to be due to the
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