Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates in the human urinary trypsin inhibitor isolated by affinity chromatography.
The inhibitory active part of the inter-alpha-trypsin inhibitor with a known amino acid sequence is present as an acid-resistant inhibitor in human serum, in urine, in bronchial and in nasal mucus. The inhibitor molecule has a 50% carbohydrate content. Carbohydrate side chains are attached in two positions. One chain is linked to the polypeptide O-glycosidically via the serine residue in position 10 in the N-terminal extension peptide. The second side chain is attached N-glycosidically via the asparagine residue in position 24, located in the inactive "inhibitory" Kunitz-type domain of the inhibitor. The composition of the carbohydrate side chains were determined.
D000510:Alpha-Globulins / Q000302:isolation & purification / Q000652:urine*; D000595:Amino Acid Sequence; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000302:isolation & purification / Q000652:urine*; D006801:Humans; D011487:Protein Conformation; D014361:Trypsin Inhibitors / Q000302:isolation & purification / Q000652:urine*
D000510:Alpha-Globulins; D002241:Carbohydrates; D006020:Glycopeptides; D006023:Glycoproteins; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor