Carbohydrate structure of human pancreatic elastase 1.

Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett. 249, 275-278]. In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.

Separation of glycoprotein-N-glycans by high-pH anion-exchange chromatography.

A series of high-mannose and complex type glycoprotein-N-glycans was subjected to high-pH anion-exchange chromatography. The results revealed that this method represents a useful tool for analytical characterization of single oligosaccharides as well as preparative separation of complex mixtures of carbohydrate side-chains. On the other hand, it became evident that in several cases a combination of different chromatographic techniques is required for efficient separation of individual oligosaccharide species.

Localization and characterization of the glycosylation site of human pancreatic elastase 1.

Crystalline elastase 1 from human pancreas was digested with trypsin. Two peptides, containing the potential N-glycosylation sites at Asn-86 and Asn-125, were isolated and analyzed by amino acid analysis, sequencing and carbohydrate component analysis. The results demonstrate that only Asn-86 is glycosylated.

Subunit III of bovine procarboxypeptidase A: its relationship to human pancreatic elastase 1.

This paper is a continuation of our study of various animal pancreatic enzymes which are related to human pancreatic elastase 1 (Sziegoleit, A. & Linder, D. (1986) Biol.