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The proteoglycan bikunin has a defined sequence
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DOI：10.1038/nchembio.673.png)
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Abstract
En 中文
Proteoglycans are complex glycoconjugates that regulate critical biological pathways in all higher organisms. Bikunin, the simplest proteoglycan, with a single glycosaminoglycan chain, is a serine protease inhibitor used to treat acute pancreatitis. Unlike nucleic acids and proteins, whose synthesis is template driven, Golgi-synthesized glycosaminoglycans are not believed to have predictable or deterministic sequences. Bikunin peptidoglycosaminoglycans were prepared and fractionated to obtain a collection of size-similar and charge-similar chains. Fourier transform mass spectral analysis identified a small number of parent molecular ions corresponding to monocompositional peptidoglycosaminoglycans. Fragmentation using collision-induced dissociation unexpectedly afforded a single sequence for each monocompositional parent ion, unequivocally demonstrating the presence of a defined sequence. The biosynthetic pathway common to all proteoglycans suggests that even more structurally complex proteoglycans, such as heparan sulfate, may have defined sequences, requiring a readjustment in the understanding of information storage in complex glycans.
Keywords:
ALPHA-TRYPSIN INHIBITOR
CHONDROITIN SULFATE OLIGOSACCHARIDES
ELECTRON DETACHMENT DISSOCIATION
COVALENTLY CROSS-LINKS
HEPARAN-SULFATE
HUMAN PLASMA
GLYCOSAMINOGLYCAN OLIGOSACCHARIDES
STRUCTURAL-ANALYSIS
ANTITHROMBIN-III
MASS-SPECTRA
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