Lenarcic B, Ritonja A, Dolenc I, Stoka V, Berbic S, Pungercar J, Strukelj B, Turk V
Department of Biochemistry and Molecular Biology, J. Stefan Institute, Ljubljana, Slovenia.
FEBS Lett. 1993 Dec 27;336(2):289-92. doi: 10.1016/0014-5793(93)80822-c.
A new stefin type low-M(r) cysteine proteinase inhibitor (PLCPI) was isolated from pig polymorphonuclear leukocytes as a contaminant of the cathelin sample. The inhibitor consists of 103 amino acids, and its M(r) was calculated to be 11,768. The inhibitor exhibits considerable sequence identity with inhibitors from the stefin family, particularly with human stefin A. The PLCPI is a fast acting inhibitor of papain and cathepsins L and S (k(ass) > or = 1 x 10(6) M-1 x s-1) and forms very tight complexes with these enzymes (Ki < or = 190 pM). The affinity for cathepsins B and H (Ki > or = 125 nM) was lower. These results also show that the inhibitory activity previously ascribed to cathelin was due to the presence of PLCPI.
