Carbohydrate as covalent crosslink in human inter‐α‐trypsin inhibitor: A novel plasma protein structure
- 28 March 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 230 (1-2) , 195-200
- https://doi.org/10.1016/0014-5793(88)80670-7
Abstract
The primary structure of inter‐α‐trypsin inhibitor is partially elucidated, but controversy about the construction of the polypeptide backbone still exists. We present evidence suggesting that inter‐α‐trypsin inhibitor represents a novel plasma protein structure with two separate polypeptide chains covalently crosslinked only by carbohydrate (chondroitin sulphate)Keywords
This publication has 16 references indexed in Scilit:
- Mechanism of action of inter-.alpha.-trypsin inhibitorBiochemistry, 1987
- The Effect of the Glycosaminoglycan Chain Removal on some Properties of the Human Urinary Trypsin InhibitorBiological Chemistry Hoppe-Seyler, 1987
- cDNA Cloning of Human Inter-α-Trypsin Inhibitor Discloses Three Different ProteinsBiological Chemistry Hoppe-Seyler, 1987
- The major human urinary trypsin inhibitor is a proteoglycanEuropean Journal of Biochemistry, 1986
- The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-α-trypsin inhibitor also encodes α-1-microgiobulin (protein HCNucleic Acids Research, 1986
- Human Inter-alpha-Trypsin-Inhibitor: Characterization and partial nucleotide sequencing of a light chain-encoding cDNABiochemical and Biophysical Research Communications, 1985
- Human Inter-α-Trypsin Inhibitor: Localization of the Kunitz-Type Domains in the N-terminal Part of the Molecule and their Release by a Trypsin-Like ProteinaseBiological Chemistry Hoppe-Seyler, 1985
- Crossed Immunoelectrophoresis as Modified for Quantitative PurposesScandinavian Journal of Immunology, 1983
- Inter‐alpha‐trypsin‐inhibitor (ITI): two distinct mRNAs in baboon liver argue for a discrete synthesis of ITI and ITI derivativesFEBS Letters, 1983
- [66]The inter-α-trypsin inhibitorPublished by Elsevier ,1976