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19924

Sigma-Aldrich

Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant from E. coli

7-13 mU (per vial)

Sinónimos:

Pyrase, Pyroglutamyl-Peptidase I, Pyrrolidone Carboxyl Peptidase

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About This Item

Número de CAS:
9075-21-2
Comisión internacional de enzimas:
3.4.19.3 (BRENDA, IUBMB)
EC Number:
232-981-8
MDL number:
MFCD00132139
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

100

form

lyophilized

specific activity

7-13 mU (per vial)

mol wt

Mr ~28000

storage temp.

−20°C

Categorías relacionadas

Packaging

package of 0.01 Unit

Unit Definition

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol Pyroglutamate-p-nitroanilide per minute at pH 7.0 and 37 °C

Analysis Note

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+.

Other Notes

An enzyme that removes pyroglutamic acid (pGlu) from pGlu-peptide and proteins; employed in Edman degradation.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_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
An Staes et al.
Proteomics, 8(7), 1362-1370 (2008-03-05)
We previously described a proteome-wide, peptide-centric procedure for sorting protein N-terminal peptides and used these peptides as readouts for protease degradome and xenoproteome studies. This procedure is part of a repertoire of gel-free techniques known as COmbined FRActional DIagonal Chromatography
William E Werner et al.
Analytical biochemistry, 342(1), 120-125 (2005-06-17)
Typically, the removal of pyroglutamate from the protein chains of immunoglobulins with the enzyme pyroglutamate aminopeptidase requires the use of chaotropic and reducing agents, quite often with limited success. This article describes a series of optimization experiments using elevated temperatures
A C Awadé et al.
Proteins, 20(1), 34-51 (1994-09-01)
Pyrrolidone carboxyl peptidase (EC 3.4.11.8) is an exopeptidase commonly called PYRase, which hydrolytically removes the pGlu-proteins. pGlu also known as pyrrolidone carboxylic acid may occur naturally by an enzymatic procedure or may occur as an artifact in proteins or peptides.
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