Isolation and Serine Protease Inhibitory Activity of the 44-Residue, C-Terminal Fragment of αl-Antitrypsin from Human Placenta
MA Niemann, AJ Narkates, EJ Miller - Matrix, 1992 - Elsevier
Abstract αl-Antitrypsin (AAT) is a potent fluid-phase inhibitor of serine proteases. It forms a
tightly bound, stoichiometric complex with these enzymes and is inactivated by cleavage
within its reactive center. Evidence is here presented, that the 44-residue C-terminal
fragment of AAT, termed SPAAT (short peptide from AAT), is found in human tissue, where it
is apparently bound to the extracellular matrix (ECM). The identity of SPAAT was established
by amino acid sequence analysis through its 40 N-terminal residues. Placental SPAAT …
tightly bound, stoichiometric complex with these enzymes and is inactivated by cleavage
within its reactive center. Evidence is here presented, that the 44-residue C-terminal
fragment of AAT, termed SPAAT (short peptide from AAT), is found in human tissue, where it
is apparently bound to the extracellular matrix (ECM). The identity of SPAAT was established
by amino acid sequence analysis through its 40 N-terminal residues. Placental SPAAT …