Activation of human pepsinogens

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 to...

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Veröffentlicht in:	FEBS letters 1988-12, Vol.241 (1), p.69-72
1. Verfasser:	Foltmann, B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Activation Amino Acid Sequence Amino acid sequencing Analytical, structural and metabolic biochemistry Biological and medical sciences Enzyme Activation Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gastric Mucosa - enzymology Humans Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Lyases Molecular Sequence Data Pepsinogen Pepsinogens - isolation & purification Pepsinogens - metabolism PgA, pepsinogen A (EC 3.4.23.1) SDS-PAGE, SDS-polyacrylamide gel electrophoresis
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Beschreibung
Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(88)81033-0