Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor.
Journal Article (Journal Article)
The human blood protein pre-alpha-inhibitor is composed of one heavy and one light protein chain. The chains are covalently linked to each other by a structure that has not previously been described, which we designate a protein-glycosaminoglycan-protein (PGP) cross-link. A combination of protein and carbohydrate analytical techniques indicates that the interchain linkage is mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to Ser-10 of the light chain. The heavy chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain. This PGP cross-link may be present in other proteins, but could have been overlooked due to the heterogeneous behavior of proteins containing glycosaminoglycan.
Full Text
Duke Authors
Cited Authors
- Enghild, JJ; Salvesen, G; Hefta, SA; Thøgersen, IB; Rutherfurd, S; Pizzo, SV
Published Date
- January 15, 1991
Published In
Volume / Issue
- 266 / 2
Start / End Page
- 747 - 751
PubMed ID
- 1898736
International Standard Serial Number (ISSN)
- 0021-9258
Language
- eng
Conference Location
- United States