Inhibition of human serine proteases by SPAAT, the C-terminal 44-residue peptide from α1-antitrypsin
MA Niemann, JE Baggott, EJ Miller - Biochimica et Biophysica Acta (BBA) …, 1997 - Elsevier
SPAAT has previously been shown to be a competitive inhibitor of the model serine
protease, chymotrypsin. We now present evidence that SPAAT is likewise a competitive
inhibitor of human neutrophil elastase and cathepsin G with Ki's of 15–20 and 40 μM,
respectively. The mechanism of this inhibition was investigated by comparing the relative
effectiveness of the 23-residue N-terminal fragment of SPAAT (N-SPAAT) to inhibit
chymotrypsin and human neutrophil elastase. N-SPAAT, which does not contain the primary …
protease, chymotrypsin. We now present evidence that SPAAT is likewise a competitive
inhibitor of human neutrophil elastase and cathepsin G with Ki's of 15–20 and 40 μM,
respectively. The mechanism of this inhibition was investigated by comparing the relative
effectiveness of the 23-residue N-terminal fragment of SPAAT (N-SPAAT) to inhibit
chymotrypsin and human neutrophil elastase. N-SPAAT, which does not contain the primary …