77152
Pepsin from porcine gastric mucosa
2× cryst., lyophilized, powder, ≥2400 U/mg
Synonym(s):
Pepsin A, Pepsin from hog stomach
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About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
42010127
EC Number:
232-629-3
MDL number:
form
powder
quality
2× cryst., lyophilized
specific activity
≥2400 U/mg
mol wt
35 kDa
UniProt accession no.
Gene Information
pig ... LOC396892(396892)
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Application
Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.
Biochem/physiol Actions
Preferential cleavage: hydrophobic and aromatic residues in P1 and P1′ postitions. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin
Analysis Note
Optimum pH is 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH 8.0 - 8.5.
Other Notes
1 U corresponds to the amount of enzyme which increases the absorbance at 280 nm by 0.001 per minute at pH 2.0 and 37°C (Hemoglobin, Cat. No. 51290, as substrate) 15′000 absorbance-U as described above are equivalent to ∼1 Bergmeyer-U. 1 Bergmeyer-U is the amount of enzyme which hydrolyzes 1 μmol Acetyl-L-phenyl-3,5-diiodo-L-tyrosine at pH 2.0 and 37°C
Sales restrictions may apply
Standard for serum pepsinogen determination; Substrate specificity; Limited hydrolysis of myelin basic protein
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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K. Morihara et al.
Proteinases and their inhibitors, V. Turk et al., eds.,, 213-213 (1981)
R E Martenson et al.
Journal of neurochemistry, 37(6), 1497-1508 (1981-12-01)
Treatment of rabbit myelin basic protein component 1 with pepsin (enzyme:substrate, 1:500 w/w) in 0.5 M-ammonium formate (pH 6.00) for 15-20 min at room temperature resulted in limited cleavage of the protein. The resulting fragments were isolated by ion-exchange chromatography
J D Harvey-White et al.
American journal of veterinary research, 43(7), 1317-1320 (1982-07-01)
A simplification of the traditional hemoglobin methods for determining serum pepsinogen concentration was developed. In this method, 10% trichloroacetic acid solution was added to control samples, and hemoglobin substrate was added to controls and active enzyme samples; standards and samples
Chuan-Hsiao Han et al.
Food chemistry, 138(2-3), 923-930 (2013-02-16)
Our previous report showed that yam dioscorin and its peptic hydrolysates exhibit radical scavenging activities; however, the functions of these peptic hydrolases are still under investigation. In this study, the thiol-containing peptides derived from computer-aided simulation of pepsin hydrolysis of
Mahmoud S Ali et al.
The Laryngoscope, 123(2), 434-439 (2012-10-17)
To assess if, as previously reported in the literature, bile acids inhibit pepsin activity, resulting in pepsin having a less important role in laryngopharyngeal damage in reflux disease. Prospective translational research study. A total of 78 patient's fasting gastric juice
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