Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure
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Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor : a novel plasma protein structure. / Jessen, T E; Faarvang, K L; Ploug, M.
In: FEBS Letters, Vol. 230, No. 1-2, 28.03.1988, p. 195-200.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor
T2 - a novel plasma protein structure
AU - Jessen, T E
AU - Faarvang, K L
AU - Ploug, M
PY - 1988/3/28
Y1 - 1988/3/28
N2 - 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).
AB - 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).
KW - Alpha-Globulins
KW - Amino Acid Sequence
KW - Carbohydrates
KW - Chondroitin Lyases
KW - Chondroitin Sulfates
KW - Chromatography, Gel
KW - Electrophoresis, Polyacrylamide Gel
KW - Humans
KW - Hyaluronoglucosaminidase
KW - Immunoelectrophoresis
KW - Immunosorbent Techniques
KW - Molecular Sequence Data
KW - Molecular Weight
KW - Trypsin Inhibitors
KW - Journal Article
M3 - Journal article
C2 - 2450785
VL - 230
SP - 195
EP - 200
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 1-2
ER -
ID: 178214818