Title : 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
Abstract :
- 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 com position of the carbohydrate side chains were determined