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Original Article

Purification of the pepsinogen A isozymogens by means of high resolution ion-exchange chromatography. Evidence for post-translational modifications

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Pages 649-655 | Received 16 Nov 1984, Accepted 20 May 1985, Published online: 08 Jul 2009
 

Abstract

Défize J, Pals G, Pronk JC, Frants RR, Rimmelzwaan G, Westerveld BD, Eriksson AW. Purification of the pepsinogen A isozymogens by means of high resolution ion-exchange chromatography. Evidence for post-translational modifications. Scand J Clin Lab Invest 1985; 45: 649-655.

Total human pepsinogen (PG) was isolated from gastric fundic mucosa and PGA (formerly called PGI) from urine, using standard ion-exchange and gel filtration techniques. Gastric PGA was separated from PGC (formerly called PGII) either by immunoaffinity or high resolution ion-exchange chromatography (fast protein liquid chromatography, Pharmacia, Uppsala, Sweden). The individual PGA isozymogens 2, 3, 4 and 5 could be isolated to homogeneity with the aid of the same ion-exchanger. Evidence was obtained for the existence of secondary modifications of the PGA fractions 3, 4 and 5, electrophoretically overlapping the primary (genetic) isozymogens.

Total human pepsinogen (PG) was isolated from gastric fundic mucosa and PGA (formerly called PGI) from urine, using standard ion-exchange and gel filtration techniques. Gastric PGA was separated from PGC (formerly called PGII) either by immunoaffinity or high resolution ion-exchange chromatography (fast protein liquid chromatography, Pharmacia, Uppsala, Sweden). The individual PGA isozymogens 2, 3, 4 and 5 could be isolated to homogeneity with the aid of the same ion-exchanger. Evidence was obtained for the existence of secondary modifications of the PGA fractions 3, 4 and 5, electrophoretically overlapping the primary (genetic) isozymogens.

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