AbstractCystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cysteine proteinases than the intact inhibitor. Such truncation of cystatin C is recorded after action of glycyl endopeptidase and cathepsin L. Incubation of cystatin C with papain, cathepsin B or cathepsin H led to no changes in the cystatin C molecule. Isoelectric focusing of the cathepsin L and cystatin C mixture showed the formation of two new bands. One of them appeared whether E-64 or PMSF was added or not, evidently representing a cystatin C/cathepsin L complex. The other band is the truncated cystatin C molecule. N-terminal sequencing after separation by HPLC showed that cystatin C is cleaved by cathepsin L at the Gly11-Gly12 bond. The ac...
AbstractFor study of the inhibition mechanism of the cystatin superfamily, cystatin A artificial mut...
AbstractA papain inhibitor or 22 kDa was isolated from human placenta and shown to be identical to r...
AbstractHuman cystatin C, a powerful physiological protein inhibitor of cathepsins B, H and L, conta...
AbstractCystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cyst...
Leucocyte elastase in catalytic amounts was observed to rapidly cleave the Val-10-Gly-11 bond of the...
We used site-directed mutagenesis to alter the specificity of human cystatin C, an inhibitor with a ...
Human cystatin C variants in which the evolutionarily conserved Gly-11 residue has been replaced by ...
AbstractCystatins A and C were both shown to inhibit cathepsin B by a two-step mechanism, involving ...
AbstractStopped-flow kinetics showed that the inhibition of the lysosomal cysteine proteinase, cathe...
The structural basis for the biological specificity of human cystatin C has been investigated. Cysta...
Human cystatin A was shown to bind rapidly and strongly to papain and cathepsin L, with Åj of 0.2-20...
Peptide segments derived from consensus sequences of the inhibitory site of cystatins, the natural i...
Human cystatins C and D share almost identical primary structures of two out of the three segments p...
The interactions between wild-type or mutant recombinant forms of human cystatin C and rat cathepsin...
Cystatin A, a mammalian cysteine proteinase inhibitor, was expressed in a bacterial system. The puri...
AbstractFor study of the inhibition mechanism of the cystatin superfamily, cystatin A artificial mut...
AbstractA papain inhibitor or 22 kDa was isolated from human placenta and shown to be identical to r...
AbstractHuman cystatin C, a powerful physiological protein inhibitor of cathepsins B, H and L, conta...
AbstractCystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cyst...
Leucocyte elastase in catalytic amounts was observed to rapidly cleave the Val-10-Gly-11 bond of the...
We used site-directed mutagenesis to alter the specificity of human cystatin C, an inhibitor with a ...
Human cystatin C variants in which the evolutionarily conserved Gly-11 residue has been replaced by ...
AbstractCystatins A and C were both shown to inhibit cathepsin B by a two-step mechanism, involving ...
AbstractStopped-flow kinetics showed that the inhibition of the lysosomal cysteine proteinase, cathe...
The structural basis for the biological specificity of human cystatin C has been investigated. Cysta...
Human cystatin A was shown to bind rapidly and strongly to papain and cathepsin L, with Åj of 0.2-20...
Peptide segments derived from consensus sequences of the inhibitory site of cystatins, the natural i...
Human cystatins C and D share almost identical primary structures of two out of the three segments p...
The interactions between wild-type or mutant recombinant forms of human cystatin C and rat cathepsin...
Cystatin A, a mammalian cysteine proteinase inhibitor, was expressed in a bacterial system. The puri...
AbstractFor study of the inhibition mechanism of the cystatin superfamily, cystatin A artificial mut...
AbstractA papain inhibitor or 22 kDa was isolated from human placenta and shown to be identical to r...
AbstractHuman cystatin C, a powerful physiological protein inhibitor of cathepsins B, H and L, conta...