AbstractHuman high- and low-Mr kininogens were shown to be potent inhibitors of cysteine proteinases such as cathepsin L and papain (Ki = 17–48 pM). A strong immunological cross-reaction between the kininogens and low-Mr α-cysteine proteinase inhibitor from human plasma was found. Comparison of partial amino acid sequences from high- and low-Mr kininogen and low-Mr α-cysteine proteinase inhibitor demonstrated sequence identity for all segments analyzed. These findings suggest that the kininogens and the α-cysteine proteinase inhibitors from human plasma are identical proteins
High Mr kininogen increases the activation rate of prekallikrein by activated factor XII on a surfac...
AbstractHMrα2CPI was found to be an inhibitor of human liver cathepsin H by the measurement of the d...
AbstractA new stefin type low-Mr, cysteine proteinase inhibitor (PLCPI) was isolated from pig polymo...
AbstractHuman high- and low-Mr kininogens were shown to be potent inhibitors of cysteine proteinases...
AbstractFluorescence titrations showed that high-molecular-weight kininogen binds two molecules of p...
We point out that human low-Mr kininogen contains three cystatin-like sequences, rather than two, as...
AbstractThe amidolytic activities of papain and rat liver cathepsins B, H and L were strongly inhibi...
AbstractThe internal domain 3 of the heavy chain of human kininogen, a cysteine proteinase inhibitor...
Murine monoclonal antibodies against the major cysteine proteinase inhibitors of human biological fl...
AbstractA papain inhibitor or 22 kDa was isolated from human placenta and shown to be identical to r...
AbstractThe calpain-binding domain 2 of the kininogens, the major plasma inhibitors of cysteine prot...
The isolation and characterization of six human cysteine proteinase inhibitors is reported. Their di...
AbstractA model for the evolution of mammalian cysteine proteinase inhibitors has been constructed o...
Six cysteine proteinase inhibitors were isolated from human urine by affinity chromatography on inso...
The amino acid sequence of the acrosin-trypsin inhibitor HUSI-II from human seminal plasma is presen...
High Mr kininogen increases the activation rate of prekallikrein by activated factor XII on a surfac...
AbstractHMrα2CPI was found to be an inhibitor of human liver cathepsin H by the measurement of the d...
AbstractA new stefin type low-Mr, cysteine proteinase inhibitor (PLCPI) was isolated from pig polymo...
AbstractHuman high- and low-Mr kininogens were shown to be potent inhibitors of cysteine proteinases...
AbstractFluorescence titrations showed that high-molecular-weight kininogen binds two molecules of p...
We point out that human low-Mr kininogen contains three cystatin-like sequences, rather than two, as...
AbstractThe amidolytic activities of papain and rat liver cathepsins B, H and L were strongly inhibi...
AbstractThe internal domain 3 of the heavy chain of human kininogen, a cysteine proteinase inhibitor...
Murine monoclonal antibodies against the major cysteine proteinase inhibitors of human biological fl...
AbstractA papain inhibitor or 22 kDa was isolated from human placenta and shown to be identical to r...
AbstractThe calpain-binding domain 2 of the kininogens, the major plasma inhibitors of cysteine prot...
The isolation and characterization of six human cysteine proteinase inhibitors is reported. Their di...
AbstractA model for the evolution of mammalian cysteine proteinase inhibitors has been constructed o...
Six cysteine proteinase inhibitors were isolated from human urine by affinity chromatography on inso...
The amino acid sequence of the acrosin-trypsin inhibitor HUSI-II from human seminal plasma is presen...
High Mr kininogen increases the activation rate of prekallikrein by activated factor XII on a surfac...
AbstractHMrα2CPI was found to be an inhibitor of human liver cathepsin H by the measurement of the d...
AbstractA new stefin type low-Mr, cysteine proteinase inhibitor (PLCPI) was isolated from pig polymo...