Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure
Research output: Contribution to journal › Journal article › Research › peer-review
The primary structure of inter-alpha-trypsin inhibitor is partially elucidated, but controversy about the construction of the polypeptide backbone still exists. We present evidence suggesting that inter-alpha-trypsin inhibitor represents a novel plasma protein structure with two separate polypeptide chains covalently crosslinked only by carbohydrate (chondroitin sulphate).
| Original language | English |
|---|---|
| Journal | FEBS Letters |
| Volume | 230 |
| Issue number | 1-2 |
| Pages (from-to) | 195-200 |
| Number of pages | 6 |
| ISSN | 0014-5793 |
| Publication status | Published - 28 Mar 1988 |
- Alpha-Globulins, Amino Acid Sequence, Carbohydrates, Chondroitin Lyases, Chondroitin Sulfates, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Humans, Hyaluronoglucosaminidase, Immunoelectrophoresis, Immunosorbent Techniques, Molecular Sequence Data, Molecular Weight, Trypsin Inhibitors, Journal Article
Research areas
ID: 178214818