Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, VII. Determination of the amino-acid sequence of the trypsin-released inhibitor from bovine inter-alpha-trypsin inhibitor.
An acid-labile proteinase inhibitor, quite similar to human inter-alpha-trypsin inhibitor, was isolated from bovine serum. An acid-resistant 30-kDa inhibitor, exhibiting properties similar to human HI-30, was also isolated. Upon limited proteolysis of both bovine inhibitors, active 14-kDa domains are released which are identical with respect to molecular mass and acid resistance. The amino-acid sequence determination of these fragments revealed a strong homology to the corresponding human inhibitor HI-14 which is characterized by two covalently linked Kunitz-type domains. The reactive-site residue is leucine in the N-terminal domain (in the human inhibitor methionine) and arginine in the C-terminal domain in both bovine and human inhibitor.
D000510:Alpha-Globulins / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism; D006801:Humans; D005779:Immunodiffusion; D007930:Leucine; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011480:Protease Inhibitors / Q000097:blood*; D013045:Species Specificity; D014357:Trypsin / Q000378:metabolism; D014360:Trypsin Inhibitor, Kunitz Soybean; D014361:Trypsin Inhibitors
D000510:Alpha-Globulins; D010446:Peptide Fragments; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor; D014360:Trypsin Inhibitor, Kunitz Soybean; D001120:Arginine; D002918:Chymotrypsin; D014357:Trypsin; D007930:Leucine