Abstract
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 |
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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 |
Keywords
- 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