z-logo
Premium
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)

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here