AbstractHuman cystatin C, a powerful physiological protein inhibitor of cathepsins B, H and L, contains two disulphide bridges, at least one of which is essential to its inhibitory activity. The positions of these bridges in the single polypeptide chain of the protein have been determined by diagonal paper electrophoresis. The cysteine residues at positions 73 and 83 form one bridge, and those at positions 97 and 117 form the other. In the homologous cystatin of chicken egg-white, the disulphides are Cys 71–Cys 81, and Cys 95–Cys 115
AbstractCystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cyst...
Six different cysteine proteinase inhibitors (cystatins) were isolated from human urine and characte...
We used site-directed mutagenesis to alter the specificity of human cystatin C, an inhibitor with a ...
AbstractHuman cystatin C, a powerful physiological protein inhibitor of cathepsins B, H and L, conta...
An alignment/phylogeny of the papain superfamily of cysteine proteases was created from which the ex...
Leucocyte elastase in catalytic amounts was observed to rapidly cleave the Val-10-Gly-11 bond of the...
AbstractThe last decade has witnessed enormous progress of protein inhibitors of cysteine proteinase...
AbstractCathepsin C was purified from human spleen by a rapid procedure, which included homogenizati...
AbstractPeptide maps obtained by reversed-phase HPLC of tryptic digests of isoelectric form 1 (pI=6....
Human cystatins C and D share almost identical primary structures of two out of the three segments p...
The structural basis for the biological specificity of human cystatin C has been investigated. Cysta...
A previously undescribed human member of the cystatin superfamily called cystatin F has been identif...
AbstractQuail cystatin, a new cysteine proteinase inhibitor protein of the cystatin superfamily, was...
The binding of human cystatin A to papain-like proteinases was quantified with a recombinant inhibit...
AbstractFive recombinant hairpin loop variants of chicken cystatin (ΔV55, ΔV55-S56, ΔP103-L105, ΔI10...
AbstractCystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cyst...
Six different cysteine proteinase inhibitors (cystatins) were isolated from human urine and characte...
We used site-directed mutagenesis to alter the specificity of human cystatin C, an inhibitor with a ...
AbstractHuman cystatin C, a powerful physiological protein inhibitor of cathepsins B, H and L, conta...
An alignment/phylogeny of the papain superfamily of cysteine proteases was created from which the ex...
Leucocyte elastase in catalytic amounts was observed to rapidly cleave the Val-10-Gly-11 bond of the...
AbstractThe last decade has witnessed enormous progress of protein inhibitors of cysteine proteinase...
AbstractCathepsin C was purified from human spleen by a rapid procedure, which included homogenizati...
AbstractPeptide maps obtained by reversed-phase HPLC of tryptic digests of isoelectric form 1 (pI=6....
Human cystatins C and D share almost identical primary structures of two out of the three segments p...
The structural basis for the biological specificity of human cystatin C has been investigated. Cysta...
A previously undescribed human member of the cystatin superfamily called cystatin F has been identif...
AbstractQuail cystatin, a new cysteine proteinase inhibitor protein of the cystatin superfamily, was...
The binding of human cystatin A to papain-like proteinases was quantified with a recombinant inhibit...
AbstractFive recombinant hairpin loop variants of chicken cystatin (ΔV55, ΔV55-S56, ΔP103-L105, ΔI10...
AbstractCystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cyst...
Six different cysteine proteinase inhibitors (cystatins) were isolated from human urine and characte...
We used site-directed mutagenesis to alter the specificity of human cystatin C, an inhibitor with a ...