Volume 6 Number 3, May/June 1996, pp.168-173
Glycobiology: the technologies associated with
Andrew A. Gooley, Anthony Pisano, Nicolle H. Packer, John W.
Redmond, Warren Kett and Keith L. Williams
Code Number: AU96003
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Protein glycosylation is ubiquitous being found on molecules
in both eukaryotes and to an increasing extent prokaryotes.
Why are proteins modified with sugars? One general
consequence for glycosylation on proteins is that the
glycosylation imparts proteinase resistance. There are
numerous examples of glycoprotein instability following the
site directed metagenesis of a glycosylation site on proteins
such as the GLYT1 glucose transporter protein, Human
transferrin receptor and the angiotensin-converting enzyme,
all expressed in chinese hamster ovary cells. However,
increasingly glycosylation on proteins has been found to be
important for protein trafficking, biological activity,
cell-cell and cell-extracellular matrix interactions (Varki,
1993). The broad interest in the structure and function of
glycoproteins has led to a relatively new discipline,
glycobiology. The principal aim of glycobiology is to
understand the structure and function of the carbohydrate
attached to a variety of carriers including protein
(glycoproteins, proteoglycans), lipid (lipopolysaccharides,
glycolipids) and to protein and lipid (glycophosphatidyl
inositol protein anchors, lipopeptidophosphoglycans).
Understanding glycosylation patterns is also of relevance to
recombinant protein design where it is desirable to engineer
glycoproteins with a variety of physio-chemical properties
including proteolytic stability, thermostability,
elasto-viscosity and structural modulation of receptors (Dwek
et al. 1993).
Copyright 1996 Australian Biotechnology Association Ltd.