Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure.
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).
D000510:Alpha-Globulins / Q000378:metabolism; D000595:Amino Acid Sequence; D002241:Carbohydrates; D002808:Chondroitin Lyases / Q000378:metabolism; D002809:Chondroitin Sulfates; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006821:Hyaluronoglucosaminidase / Q000378:metabolism; D007122:Immunoelectrophoresis; D007163:Immunosorbent Techniques; D008969:Molecular Sequence Data; D008970:Molecular Weight; D014361:Trypsin Inhibitors
D000510:Alpha-Globulins; D002241:Carbohydrates; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor; D002809:Chondroitin Sulfates; D006821:Hyaluronoglucosaminidase; D002808:Chondroitin Lyases