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P7125 Sigma-Aldrich

Pepsin from porcine gastric mucosa

powder, ≥400 units/mg protein

Synonym: Pepsin A, Pepsin from hog stomach

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Enzyme Class Index,
Quality Level   200
form   powder
specific activity   ≥400 units/mg protein
mol wt   35 kDa
solubility   10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless
storage temp.   2-8°C
Gene Information   pig ... LOC396892(396892)

Description

Application

Pepsin is a peptidase used to digest proteins and is commonly used in the preparation of Fab fragments from antibodies. Pepsin, from porcine gastric mucosa, has been used to hydrolyze dry cervical samples in mice. Product P7125 is provided in powder form. Product P7125 has been used to denature DNA from kidney cells and to digest pathology samples from anal canal carcinomas (ACC) biopsies prior to EGFR staining.

The enzyme from Sigma has been used to obtain total vitamin B12 content in food products prior using immunoaffinity columns It has also been used to digest minced soft tissue of snails prior to the isolation of the third stage larvae (L3).

Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.

Packaging

100, 500 g in poly bottle

Biochem/physiol Actions

It does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.

Pepsin hydrolyzes peptide bonds, not amide or ester linkages. Pepsin cleaves peptides with an aromatic acid on either side of the peptide bond. Sulfur-containing amino acids increase susceptibility to hydrolysis when they are close to the peptide bond. Pepsin preferentially cleaves at the carboxyl side of phenylalanine and leucine and at the carboxyl side of glutamic acid residues. 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
Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages.

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

Unit Definition

One unit will produce a ΔA280 of 0.001 per min at pH 2.0 at 37 °C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16 mL. Light path = 1 cm.)

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.

Protein determined by E1%/280

Other Notes

View more information on pepsin at www.sigma-aldrich.com/enzymeexplorer.

Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Target organs 
Respiratory system
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 1
RTECS 
SC6132000
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

Protocols

Enzymatic Assay of Pepsin (3.4.23.1)

This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.

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