Characterization of urinary proteinase inhibitors with segments of amino acids sequences identical to sequences of pancreatic secretory trypsin inhibitor.
1. Slow migrating proteinase inhibitors were isolated from pathological human urine. 2. The N-terminal amino acid sequence including 23 amino acids was identical to the one in pancreatic secretory trypsin inhibitor. 3. The slow migrating proteinase inhibitors occurred in 3 forms with different electrophoretic mobility. 4. Time of flight mass spectrometry showed that the Mw of one of the forms was 6241 while the Mw of another form was 5923. 5. The Ki of complexes with trypsin was determined to be 1 x 10(-10) M, with chymotrypsin and plasmin Ki was 1 x 10(-7) M. Elastase, kallikrein and thrombin were not inhibited.
Odum
L
L
Department of Clinical Chemistry, Rigshospitalet, Copenhagen, Denmark.
Halkier
T
T
Højrup
P
P
Schousboe
I
I
D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D013058:Mass Spectrometry; D008875:Middle Aged; D008969:Molecular Sequence Data; D011014:Pneumonia / Q000652:urine; D011480:Protease Inhibitors / Q000302:isolation & purification / Q000652:urine*; D013379:Substrate Specificity; D013927:Thrombosis / Q000652:urine; D014359:Trypsin Inhibitor, Kazal Pancreatic; D014361:Trypsin Inhibitors; D014682:Vena Cava, Inferior
D000596:Amino Acids; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D014359:Trypsin Inhibitor, Kazal Pancreatic