title: Activation of human pepsinogens.
abstract: Human pepsinogen A3 and A5 have been purified to chromatographic and electrophoretic homogeneity. At pH 2 pepsinogen A3 activates at a much faster rate than pepsinogen A5. Leu-23-Lys-24 is the first bond cleaved during activation of pepsinogen A3. This bond is also cleaved in pepsinogen A5, but together with the cleavage of Asp-25-Phe-26. Amino acid sequencing shows that pepsinogen A3 has Glu at position 43, whereas pepsinogen A5 has Lys.
authors.affiliation: Institute of Biochemical Genetics, University of Copenhagen, Denmark.
authors.forename: B
authors.initials: B
authors.lastname: Foltmann
mesh_terms: D000595:Amino Acid Sequence; D004789:Enzyme Activation; D005753:Gastric Mucosa / Q000201:enzymology; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010435:Pepsinogens / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D007527:Isoenzymes; D010435:Pepsinogens