Agar gel electrophoresis of proteolytic enzymes in gastric juice of patients with chronic gastritis

Agunod, Mona; Glass, George B. Jerzy

doi:10.1007/bf02231153

Cited by 3 publications

(1 citation statement)

References 33 publications

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“…However, the individuality and significance of the more electrophoretically mobile pepsins 1 and 2 have been regarded by some with suspicion. For example, Agunod & Glass (1972) and Whitecross et al (1974) suggested that the latter enzymes were evidence of breakdown products of a larger enzyme, formed in the gastric juice. The evidence from the preparative studies now reported clearly suggests that the enzymes labelled 1 and 2 do have a definite identity and are therefore separate enzymes.…”

Section: Individual Pepsinsmentioning

confidence: 99%

The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose

Roberts¹,

Taylor²

1978

Biochemical Journal

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A procedure was devised for isolating human pepsins 1, 2, 3 and 5 from gastric juice by repetitive column chromatography on DEAE-cellulose. The combined yields in four different experiments varied from 14% to 90% of the total peptic activity of the starting material. The isolated individual pepsins were shown to behave as single homogeneous proteins on agar-gel electrophoresis at pH 5.0 and on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. There is preliminary evidence, requiring further study, of two other pepsins, one migrating between pepsins 1 and 2 and the other a pepsin-3 component associating closely with pepsin 5 on chromatography.

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Section: Individual Pepsinsmentioning

confidence: 99%

The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose

Roberts¹,

Taylor²

1978

Biochemical Journal

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Simultaneous electrophoresis of pepsinogens and pepsins

1973

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Agarelektrophoretische Darstellung der proteolytischen Aktivität in Extrakten aus der Magenschleimhaut des Schweins

Böttger

Höller

2010

Zentralblatt Für Veterinärmedizin Reihe A

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Zusammenfassung Die proteolytischen Fraktionen in den drei verschiedenen Schleimhaut‐typen des Schweinemagens (Fundus‐, Pylorus‐ und Cardiadrüsenzone) wurden durch Agargelelektrophorese getrennt und nach der Enzym‐Substrat‐Reaktion mit Hämoglobin auf der Gelplatte qualitativ und quantitativ dargestellt. Die direkte photometrische Ausmessung der Gelplatten führte zu Ergebnissen, die eine Beurteilung der proteolytischen Aktivität von Schleimhautextrakten auf vergleichender Basis erlauben. Alle untersuchten Extrakte ergaben zwei gut voneinander abgesetzte Pepsinogen‐Banden, die in sich jedoch nicht homogen waren, sondern Proteolyse bei mindestens zwei pH‐Optima zeigten. Aus den Aktivitätskurven im Bereich pH 1,5–5,0 geht hervor, daß in der Magenschleimhaut des Schweins mindestens zwei, wahrscheinlich aber drei Pepsine mit pH‐Optima bei pH 1,8–2,0, pH 2,0–2,2 und pH 2,8–3,2 gebildet werden, sowie ein weitgehend alkalistabiles Gastricsin mit Wirkungsoptimum bei pH 3,2–3,4. Die Aktivierung der Enzymvorstufen kann beim pH‐Optimum des Enzyms erfolgen, setzt also keine starke Ansäuerung des Mageninhalts voraus. Summary Agarelectrophoretic demonstration of proteolytic activity in extracts of the pig gastric mucosa Proteolytic fractions of the three different types of gastric mucosa of the pig (i. e. fundic, pyloric and cardiac) were separated by agar gel electrophoresis. The enzyme‐substrate reaction with hemoglobin and subsequent staining were performed directly on the plates. Direct photometric analysis of the agar plates permits quantitative assessment of the proteolytic activities though on a comparative basis only. All mucosal extracts contained two distinct zymogen fractions which, however, were not homogenous showing proteolytic activities with at least two pH optima. Proteolytic activities were studied within the range pH 1.5–5.0, and it appears that gastric mucosa of the pig contains at least two, possibly three different pepsins and one gastricsin. The pH optima were pH 1.8–2.0, pH 2.0–2.2, pH 2.8–3.2 and pH 3.2–3.4. Activation of the zymogens readily occurs at the pH optimum of the respective enzyme, thus strong acidification of gastric contents is not required for proteolytic action. Résumé Représentation par électrophorèse sur agar de l'activité protéolytique d'extraits de la muqueuse stomacale chez le porc On a séparé au moyen d'électrophorèse sur agar les fractions protéolytiques dans les trois types différents de la muqueuse stomacale du porc (zone des glandes du fond, du pylore et du cardia) et on a procédé à une mise en évidence qualitative et quantitative selon la réaction enzyme‐substrat avec hémoglobine sur plaque de gélose. La mesure photométrique directe des plaques de gélose dennèrent des résultats qui permirent un examen de l'activité protéolytique des extraits de muqueuses sur une base comparable. Tous les extraits examinés ont donné deux bandes pepsinogènes bien séparées qui n'étaient cependant pas homogènes mais qui montrèrent pour le moins une protéolyse par deux pH optima. Il résulta des courb...

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Agar gel electrophoresis of proteolytic enzymes in gastric juice of patients with chronic gastritis

Cited by 3 publications

References 33 publications

The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose

The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose

Simultaneous electrophoresis of pepsinogens and pepsins

Agarelektrophoretische Darstellung der proteolytischen Aktivität in Extrakten aus der Magenschleimhaut des Schweins

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