Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, X. The amino-acid sequences of the trypsin-released inhibitors from horse and pig inter-alpha-trypsin inhibitors.
The amino-acid sequences of the acid-resistant inhibitors released from horse and pig inter-alpha-trypsin inhibitor (ITI) by tryptic proteolysis were determined. They are composed of two covalently linked Kunitz-type domains. In both cases the reactive site of their C-terminal antitryptic domains is occupied by arginine as in the homologous human and bovine inhibitors. The reactive site of their N-terminal domain exhibits only a weak interaction with polymorphonuclear granulocytic elastase and is occupied by leucine as in the strong elastase inhibitor released from bovine ITI. The differences between inhibitory activities of the ITI-derived inhibitors from horse, pig, and cattle are discussed on the basis of sequence differences in position P'2.
Hochstrasser
K
K
Wachter
E
E
Albrecht
G J
GJ
Reisinger
P
P
D000510:Alpha-Globulins / Q000097:blood; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D006736:Horses; D007700:Kinetics; D010446:Peptide Fragments / Q000032:analysis*; D013045:Species Specificity; D013552:Swine; D014357:Trypsin; D014360:Trypsin Inhibitor, Kunitz Soybean; D014361:Trypsin Inhibitors
D000510:Alpha-Globulins; D010446:Peptide Fragments; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor; D014360:Trypsin Inhibitor, Kunitz Soybean; D002918:Chymotrypsin; D014357:Trypsin