19924
Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant from E. coli
7-13 mU (per vial)
Synonyme(s) :
Pyrase, Pyroglutamyl-Peptidase I, Pyrrolidone Carboxyl Peptidase
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About This Item
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Forme
lyophilized
Activité spécifique
7-13 mU (per vial)
Poids mol.
Mr ~28000
Température de stockage
−20°C
Catégories apparentées
Conditionnement
package of 0.01 Unit
Définition de l'unité
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol Pyroglutamate-p-nitroanilide per minute at pH 7.0 and 37 °C
Remarque sur l'analyse
enzyme activity: the optimum temperature is 95-100 °C (the enzyme is stable up to 75 °C), the optimum pH is 6-9 (stable from pH 6-9). Inhibitors: PCMB, Hg+.
Autres remarques
An enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptide and proteins; employed in Edman degradation.
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 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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J Mozdzanowski et al.
Analytical biochemistry, 260(2), 183-187 (1998-07-11)
For larger proteins, efficient deblocking prior to Edman sequencing is especially important to obtain quality, extended sequencing data which is limited by the stepwise accumulation of background from the random acid hydrolysis of the protein. Therefore, any portion that remains
Y Shimada et al.
Journal of biochemistry, 106(3), 383-388 (1989-09-01)
The cDNA clone of Geotrichum candidum (Geo.) lipase was isolated from the Geo. cDNA library by colony hybridization using 32P-labeled oligonucleotides corresponding to a partial amino acid sequence of this enzyme. The nucleotide sequence of the cDNA determined by the
Marie Schaeffer et al.
Molecular and biochemical parasitology, 150(2), 318-329 (2006-10-10)
Pyroglutamyl peptidases I (PPI) are cysteine peptidases of the clan CF, family C15, which hydrolyse N-terminal l-pyroglutamyl residues (l-pGlu). The l-pGlu modification is a post-transcriptional modification that confers relative aminopeptidase resistance and, in some cases, is essential to the modified
Johanna L Hellström et al.
Biochimica et biophysica acta, 1764(11), 1735-1740 (2006-10-20)
To enable Edman sequencing of pyroglutamylated immunoglobulins, enzymatic deblocking by pyroglutamate aminopeptidase is performed, often with variable yield and compromised solubility. Recently, enzymatic deblocking of immunoglobulins without denaturation was described. Although the conditions ensured efficient removal of pyroglutamyl residues, we
Noriko Higaki-Sato et al.
Journal of agricultural and food chemistry, 54(19), 6984-6988 (2006-09-14)
In order to determine pyroglutamic acid levels in plasma, we developed a method based on precolumn derivatization of the carboxyl group of pyroglutamic acid with 2-nitrophenylhydrazine. Eight-week-old male SD strain rats were administered 200 mg of an acidic peptide fraction
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