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Glycosylation heterogeneity of recombinant plasminogen expressed in CHO cells

Thomson, Alan, Roberts, G., Jenkins, Nigel (1995) Glycosylation heterogeneity of recombinant plasminogen expressed in CHO cells. Genietic Engineer and Biotechnologist, 15 . pp. 293-296. ISSN 0959-020X. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:19095)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.

Abstract

Plasminogen (Plg) is the zymogen form of the serine protease plasmin and has been expressed In a CHO cell line. It is a prerequisite for such recombinant human glycoproteins being produced in mammalian cell systems that then glycosylation profile is similar to the native protein secreted by the human liver. Pig exists as true glycoforms, types I and II, type I having both an N-linked glycosylation site occupied at Asn(289) and an O-linked site at Thr(346). Type II is only modified at Thr(346), despite also containing tire N-linked consensus sequence. Capillary zone electrophoresis has been used to separate both glycoforms showing the relative distribution of both types in human plasminogen. Matrix-assisted laser desorption/ionisation-time of flight mass spectrometry (MALDI-MS) has been used to determine the sugar structures on glycopeptides generated following chymotrypsin digestion of human Plg.

Item Type: Article
Uncontrolled keywords: recombinant plasminogen; glycosylation; heterogeneity; CHO cells
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: I.T. Ekpo
Date Deposited: 25 Oct 2009 10:33 UTC
Last Modified: 16 Nov 2021 09:57 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/19095 (The current URI for this page, for reference purposes)
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