Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor.
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Morelle W, Capon C, Balduyck M, Sautiere P, Kouach M, Michalski C, Fournet B, Mizon J
Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor.
Eur J Biochem. 1994 Apr 15;221(2):881-8.
- PubMed ID
- 7513643 [ View in PubMed]
- Abstract
Inter-alpha-trypsin inhibitor (ITI) is a tight complex of three different proteins: bikunin and two heavy chains H1 and H2. In order to demonstrate that the three chains are covalently linked by a chondroitin sulphate chain as previously proposed [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherford, S. and Pizzo, S. V. (1991) J. Biol. Chem. 266, 747-751], ITI was extensively digested with thermolysin and the glycosaminoglycan-containing fragment was isolated from the digest by ion-exchange chromatography. Its peptide structural determination and mass spectrometry analysis both provide evidence that the different peptide chains constituting ITI are associated by the new cross-link described as the protein-glycosaminoglycan-protein cross-link.