Biol. Chem. Hoppe-Seyler Vol. 374, pp. 385-393, June 1993 Wieslaw WATOREK", Herman van HALBEEKb*c and James TRAVisb " Institute of Biochemistry, Wroclaw University, Poland h Department of Biochemistry, The University of Georgia. USA c Complex Carbohydrate Research Center, The University of Georgia, USA (Received 1 March 726 April 1993) Summary: The two proteinases found in human neutrophil granules, elastase and cathepsin G, each are normally isolated as a mixture of isoforms differing only in carbohydrate content. Elastase has two Nglycosylation sites occupied (Asn-45 and Asn-144), whereas cathepsin G has only one (Asn-64). Analysis of a minor form of elastase (E-l) and cathepsin G (C-l) indicates that the carbohydrate structures at each glycosylation site are complex-type bi-antennary chains usually associated with secretory glycoproteins. In contrast, the isoforms E-3 and C-3, the major forms of elastase and cathepsin G respectively, contain exclusively truncated, oligomannose-type chains at the same positions in the sequence of each protein. These data suggest the possibility that certain elastase and cathepsin G isoforms (E-l and C-l) might be destined for secretory, others (E-3 and C-3) for lysosomal functions. Key terms: Elastase, cathepsin G. carbohydrate, isozyme, neutrophil. The two major proteolytic enzymes in human neutrophils, elastase (HNE)
Biological Chemistry Hoppe-Seyler – de Gruyter
Published: Jan 1, 1993
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