Isolation and partial characterization of a low molecular weight trypsin inhibitor from human urine.
A low molecular weight glycoprotein which completely inhibited trypsin at a 1 : 1 molar ratio was isolated from human urine. It was generated from a precursor molecule which in turn derived from plasma inter-alpha-trypsin inhibitor. It had one polypeptide chain with a molecular weight of about 20 000 and a high content of half-cystine residues. Its amino-terminal amino-acid sequence was Val-Thr-Glu-Val-Thr-X-Leu-Glu-Asp-.
D000510:Alpha-Globulins / Q000378:metabolism; D000595:Amino Acid Sequence; D002241:Carbohydrates / Q000032:analysis; D006023:Glycoproteins / Q000652:urine; D006801:Humans; D007122:Immunoelectrophoresis; D007684:Kidney Tubules; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011507:Proteinuria / Q000652:urine*; D014361:Trypsin Inhibitors / Q000302:isolation & purification / Q000652:urine*
D000510:Alpha-Globulins; D002241:Carbohydrates; D006023:Glycoproteins; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor