Acid-stable protease inhibiting polypeptides formed from denatured horse plasma by proteolysis.
1. Trypsin digestion of perchloric acid precipitated horse plasma yielded polypeptides with inhibitory properties for trypsin, chymotrypsin and, to a small extent, kallikrein. 2. The Mr of the inhibitory polypeptides were 73,000 and 24,000. 3. The number, enzyme specificity and Mr of the inhibitory polypeptides differed from the values known for the human being. 4. The inhibitory polypeptides were purified by affinity chromatography on Sepharose-trypsin and by gel filtration through Sephadex G-75. 5. Protease inhibitory polypeptides were generated in the same manner by chymotrypsin, elastase, proteinase K, pronase, collagenase, papain and subtilisin. 6. The number and electrophoretic migration of the inhibitory polypeptides obtained with the different enzymes were variable. 7. The enzyme specificity was constant since all polypeptides inhibited only trypsin, chymotrypsin and kallikrein to a small extent. 8. None of the inhibitory polypeptides were immunologically related to native plasma proteins or plasma protease inhibitors.
Pellegrini
A
A
Department of Veterinary Physiology, University of Zürich, Switzerland.
Hägeli
G
G
von Fellenberg
R
R
D000818:Animals; D002850:Chromatography, Gel; D004355:Drug Stability; D006736:Horses / Q000097:blood*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010455:Peptides / Q000097:blood* / Q000302:isolation & purification; D011480:Protease Inhibitors / Q000097:blood* / Q000302:isolation & purification; D011489:Protein Denaturation
D010455:Peptides; D011480:Protease Inhibitors