Author/Editor | Cimerman, Nina; Trstenjak-Prebanda, Mojca; Turk, Boris; Popovič, Tatjana; Dolenc, Iztok; Turk, Vito | |
Title | Interaction of cystatin C variants with papain and human cathepsins B,H and L | |
Type | članek | |
Source | J Enzym Inhib | |
Vol. and No. | Letnik 14 | |
Publication year | 1999 | |
Volume | str. 167-74 | |
Language | eng | |
Abstract | Recombinant human cystatin C and two of its mutants were expressed in Escherichia coli. The recombinant inhibitor was found to identical to authentic cystatin C as judged by isoelectric focusing (pI 9.2) and kinetics of inhibition of papain and human cathepsins B, H and L. N-terminal truncation of 8 residues resulted in a decrease of isoelectric point (pI 7.8), but the inhibitory properties were similar to those of recombinant cystatin C, suggesting that Leu9 is a critical residue for the inhibition. The mutation of Trp106 to Ser, however, resulted in a decreased affinity of the inhibitor for the enzymes tested, with the largest effect on cathepsin B inhibition (100-fold in increase in Ki). | |
Descriptors | CYSTATINS CATHEPSIN B ENZYME INHIBITORS PAPAIN BACTERIAL PROTEINS ESCHERICHIA COLI PROTEINS |