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Carbohydrate as covalent crosslink in human inter‐α‐trypsin inhibitor: A novel plasma protein structure
Author(s) -
Jessen Torben E.,
Faarvang Karen L.,
Ploug Michael
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80670-7
Subject(s) - chemistry , trypsin , covalent bond , trypsin inhibitor , human plasma , carbohydrate , biochemistry , enzyme , chromatography , organic chemistry
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)