@article{ab099d1e11a443468bdf50909e5a17d3,
title = "Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure",
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).",
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",
author = "Jessen, {T E} and Faarvang, {K L} and M Ploug",
year = "1988",
month = mar,
day = "28",
language = "English",
volume = "230",
pages = "195--200",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-2",
}