Isolation of a protease inhibitor from tissues resistant to tumor invasion.
We have purified to homogeneity the major trypsin inhibitors from both bovine cartilage and aorta, two tissues reported to be highly resistant to invasion. The two inhibitors appear to be identical and they resemble the Kunitz inhibitor with respect to molecular weight, amino acid composition, range of susceptible proteases, and antigenicity. Each of these inhibitors accounts for 100% of the antitrypsin activity found in extracts of bovine cartilage and aorta.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000032:analysis*; D002356:Cartilage / Q000032:analysis*; D002417:Cattle; D008970:Molecular Weight; D011480:Protease Inhibitors; D014360:Trypsin Inhibitor, Kunitz Soybean; D014361:Trypsin Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology
D000596:Amino Acids; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D014360:Trypsin Inhibitor, Kunitz Soybean