Comparative properties of three functionally different but structurally related serpin variants from horse plasma.
Three structurally related but functionally different serpins from horse plasma were isolated and characterized. In spite of their identical N-terminal sequences, which show some similarity to that of human alpha 1-proteinase inhibitor, the reactive-centre loops of each of these proteins show extensive variation. Only inhibitor I, with a P1 methionine residue, resembles human alpha 1-PI with regard to (a) similarity of amino acid sequence in the vicinity of the reactive-site peptide bond, (b) broad inhibitory specificity, (c) sensitivity to oxidative inactivation and (d) high rate of reactivity with neutrophil elastase(s). Inhibitor II, with a P1 arginine residue, is an exclusive trypsin inhibitor, and inhibitor III is an oxidation-resistant slow-reacting elastase inhibitor with a P1 alanine residue. Comparison of association rate constants for the inhibition of horse neutrophil elastases by the three inhibitors indicates that only inhibitor I is likely to be physiologically important in the regulation of these enzymes.
Potempa
J
J
Institute of Molecular Biology, Jagiellonian University, Cracow, Poland.
Wunderlich
J K
JK
Travis
J
J
D000595:Amino Acid Sequence; D000818:Animals; D010450:Endopeptidases / Q000378:metabolism; D006736:Horses; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D015843:Serpins / Q000097:blood* / Q000737:chemistry / Q000302:isolation & purification
D015843:Serpins; D010450:Endopeptidases