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P6675

Sigma-Aldrich

Prolidase from porcine kidney

lyophilized powder, ≥100 units/mg protein

Sinonimo/i:

Aminoacyl-L-proline hydrolase, Imido Dipeptidase, Prolidase, Proline dipeptidase

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Forma fisica

lyophilized powder

Attività specifica

≥100 units/mg protein

Composizione

Protein, 20-74% Lowry

Temperatura di conservazione

−20°C

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Categorie correlate

Descrizione generale

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.

Applicazioni

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.

Azioni biochim/fisiol

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.

Definizione di unità

One unit will hydrolyze 1.0 μmole of Gly-Pro per min at pH 8.0 at 40 °C.

Stato fisico

Supplied as a lyophilized powder containing Tris buffer salt and MnCl2.

Pittogrammi

Health hazardExclamation mark

Avvertenze

Danger

Indicazioni di pericolo

Classi di pericolo

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

Organi bersaglio

Respiratory system

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1


Certificati d'analisi (COA)

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I clienti hanno visto anche

Mehmet A Altay et al.
Scandinavian journal of clinical and laboratory investigation, 71(7), 576-582 (2011-08-13)
We aimed to investigate serum prolidase activity and to find out its association with oxidative-antioxidative status in patients with idiopathic clubfoot and during the course of the disease. Oxidative status parameters, including total free sulfhydryl groups (-SH), total antioxidant capacity
Roberta Besio et al.
Clinica chimica acta; international journal of clinical chemistry, 412(19-20), 1814-1820 (2011-06-28)
Prolidase is a metallo-exopeptidase hydrolyzing X-Pro and X-Hyp dipeptides. Its absence or reduced level is typical in prolidase deficiency (PD) patients, and altered prolidase activity was reported in various diseases. Therefore, standardized and accurate measurement of prolidase activity is essential
Influence of transglutaminase treatment of skim milk on the formation of varepsilon-(Γ-glutamyl) lysine and the susceptibility of individual proteins towards crosslinking
Sharma R, et al.
International dairy journal, 11(10), 785-793 (2001)
Ewa Karna et al.
Molecular and cellular biochemistry, 361(1-2), 235-241 (2011-10-14)
Products of prolidase [E.C. 3.4.13.9] activity, proline or hydroxyproline, contribute to up-regulation of hypoxia-inducible factor-1α (HIF-1α). Prolidase activity is regulated by β(1)-integrin signaling. We studied the effects of echistatin (a well-known disintegrin) and thrombin (a serine protease capable of activation
Isolation and partial characterization of an antibacterial substance produced by Enterococcus faecium
Pantev A, et al.
Folia Microbiologica, 47(4), 391-400 (2002)

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