Pepsina from porcine gastric mucosa

pH óptimo es 2-4. Activa en urea 4 M y HCl de guanidina 3 M. Estable a 60 ºC. La pepsina se desactiva de manera irreversible a pH 8,0 - 8,5.

Protein determined by E1%/280

Puede utilizarse hidrólisis con pepsina para producir los fragmentos F(ab′)₂ de los anticuerpos. pepsina en www.sigma-aldrich.com/enzymeexplorer

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).

Escisión preferente: residuos hidrófobos y aromáticos en las posiciones P1 y P1′. Rompe los enlaces Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe y Phe-Tyr en la cadena β de la insulina

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.

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.)

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