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Characterization of human pepsin II obtained from purified gastric pepsinogen II

Charakterisierung von menschlichem Pepsin II gewonnen aus gereinigtem Magenpepsinogen II

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Zusammenfassung

Menschliches Pepsinogen II (PgII) wurde aus Magenschleimhautextrakten durch Immunoadsorbentien mit Hilfe von anti-PgII Antiserum isoliert. Spurensubstanzen von Pepsinogen I (PgI) wurden durch eine folgende anti-PgI Immunoadsorption entfernt. PgII wurde weiter auf DEAE-Sephadex A50 aufgetrennt. In der Agargelenzym-Electrophorese (AEE) bei pH 8,2 wurde PgII in fünf proteolytische Banden aufgetrennt. PgII wurde in Pepsin II (PII) durch die Ansäuerung bei pH 2,0 übergeführt und wurde anschließend von einem Inhibitor und von anderen Substanzen über DEAE gereinigt. Gereinigtes PII zeigte zwei proteolytische Bande in AEE bei pH 5,6 und war immunchemisch mit PgII identisch. „Gastricsin“ und „Pepsin“, die von saurem Magensaft durch klassiche Präparation hergestellt wurden, waren mit PII bzw. Pepsin I (PI) identisch. PII zeigte eine relativ breite pH-Aktivität mit einem Maximum bei pH 2,9. PII hydrolisierte in Gegensatz zu PI nicht N-Acetyl-Phenylalanyl-3,5-Diiodotyrosin und zeigte eine höhere Alkalistabilität als PI. Eine modifizierte Nomenklatur wird für das menschliche Pepsinogensystem vorgeschlagen.

Summary

Human pepsinogen II (PgII) was purified from human gastric mucosa by immunoadsorbents using anti-PgII antiserum. Contaminating pepsinogen I (PgI) was adsorbed by a subsequent anti-PgI immunoadsorbent. PgII was further purified on DEAE-Sephadex A50. By agar gel enzyme electrophoresis (AEE) at pH 8.2 PgII was separated into five proteolytic bands, demonstrated upon acidification and incubation with hemoglobin. PgII was converted to pepsin II (PII) by acidification at pH 2.0 and was immediately separated from its inhibitory peptide and from other substances by DEAE chromatography. Purified PII showed two bands in AEE at pH 5.6 and was immunochemically identical with PgII. The “gastricsin” and “pepsin” purified from acid gastric juice by classical procedures proved to be identical with PII and pepsin I (PI), respectively. PII showed a broad pH range with one maximum at pH 2.9. PII in contrast to PI did not hydrolize N-acetylphenylalanyl-3,5-diiodotyrosine and proved to be more alkali-stable than PI. A modified nomenclature is proposed for the human pepsinogen system.

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  1. Th. Becker

    Present address: Institut für Klinische Chemie Klinikum Großhadern, Marchioninistraße 15, D-8000, München 70

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  1. Institute of Nuclear Medicine, German Cancer Research Center and Medical Clinic, University of Heidelberg, Germany

    Th. Becker &  W. Rapp

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Supported in part by grants of the ‘Deutsche Forschungsgemeinschaft’

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Becker, T., Rapp, W. Characterization of human pepsin II obtained from purified gastric pepsinogen II. Klin Wochenschr 57, 719–724 (1979). https://doi.org/10.1007/BF01477553

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  • DOI: https://doi.org/10.1007/BF01477553

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