Biochemical Properties
A1AT is a single-chain glycoprotein consisting of 394 amino acids in the mature form and exhibits a number of glycoforms. The three N-linked glycosylations sites are mainly equipped with so-called diantennary N-glycans. However, one particular site shows a considerable amount of heterogeneity since tri- and even tetraantennary N-glycans can be attached to the Asparagine 107 (ExPASy amino acid nomenclature). These glycans carry different amounts of negatively-charged sialic acids, this causes the heterogeneity observed on normal A1AT when analysed by isoelectric focussing. In addition, the fucosylated triantennary N-glycans were shown to have the fucose as part of a so-called Sialyl Lewis x epitope, which could confer this protein particular protein-cell recognition properties. The single cysteine residue of A1AT in position 256 (ExPASy nomenclature) is found to be covalently linked to a free single cysteine by a disulfide bridge.
Read more about this topic: Alpha 1-antitrypsin
Famous quotes containing the word properties:
“The reason why men enter into society, is the preservation of their property; and the end why they choose and authorize a legislative, is, that there may be laws made, and rules set, as guards and fences to the properties of all the members of the society: to limit the power, and moderate the dominion, of every part and member of the society.”
—John Locke (1632–1704)