Pepsin (EC 3.4.23.1)
Advantages at a glance
- Appearance: sligthly yellow powder
- Loss on drying: <5%
- Microbiological test: <10000 cfu/g
- MW = ca. 36,000 g/mol
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Product information "Pepsin (EC 3.4.23.1)"
Pepsin from pig stomach. Its inactive precursor is the pepsinogen secreted by the main cells of the gastric mucosa. Pepsinogen is cleaved at acidic pH below 3 into the proteolytically active pepsin.
Pepsin is one of the important proteolytic enzymes in the digestive system. It is a phosphoprotein, or an endopeptidase which preferentially cleaves peptide bonds behind aromatic amino acids. The enzyme consists of 327 amino acids and has a molecular weight of about 35,000 daltons and a catalytic pH optimum of about 1.8. In non-acidic Mileu pepsin shows virtually no activity.
Specifications:
Pepsin is an aspartic endopeptidase with relatively broad specificity. Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1′ positions.
This Pepsin is a 1:10000 Pepsin with an activity of >10000 N.F. units/mg with 10000 N.F. U/mg = 10000 FCC U/mg = 1.67 U/mg USP = 1.67 U/mg Ph Eur = 1.67 U/mg FIP
Activity: min. 10000 N.F. U/mg
Appearance: sligthly yellow powder
Loss on drying: <5%
Microbiological test: <10000 cfu/g
MW = ca. 36,000 g/mol
Quelle / Source:
gastric mucosa of pigsSicherheits Hinweise / Safety
Klassifizierungen / Classification
Documents:
CertificateCategory List
Specifications:
This Pepsin is a 1:10000 Pepsin with an activity of >10000 N.F. units/mg with
10000 N.F. U/mg = 10000 FCC U/mg = 1.67 U/mg USP = 1.67 U/mg Ph Eur = 1.67 U/mg FIP
Appearance: sligthly yellow powder
Loss on drying: <5%
Microbiological test: <10000 cfu/g