| Interacting proteins: P29622 and P07339 |
Pubmed |
SVM Score :0.0 |
| It was shown that the kininogenase activity of chicken liver cathepsin D was slightly inhibited by the basic pancreatic trypsin and kallikrein inhibitor from bovine organs ( Kunitz type ) and by soya bean trypsin inhibitor . ^^^ |
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| Interacting proteins: P29622 and P07339 |
Pubmed |
SVM Score :0.0 |
| Alpha 1 antichymotrypsin and kallistatin hydrolysis by human cathepsin D . ^^^ In the present paper , we demonstrate that alpha 1 antichymotrypsin , a serpin with high inhibitory specificity toward cathepsin G , and kallistatin , a human serpin with high specificity toward tissue kallikrein , are digested by cathepsin D . ^^^ Therefore , besides the description of a new class of very efficient internally quenched substrates for cathepsin D , we give evidence for the downregulation role of this proteinase on alpha 1 antichymotrypsin and kallistatin . ^^^ |
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| Interacting proteins: P29622 and P07339 |
Pubmed |
SVM Score :0.0 |
| Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin . ^^^ Kallistatin , a serpin that specifically inhibits human tissue kallikrein , was demonstrated to be cleaved at the Phe Phe bond in its reactive site loop ( RSL ) by cathepsin D . ^^^ Internally quenched fluorescent peptides containing the amino acid sequence of kallistatin RSL were highly susceptible to hydrolysis by cathepsin D . ^^^ Due to the importance of cathepsin D in several physiological and pathological processes , we took the peptide containing kallistatin RSL sequence , Abz Ala Ile Lys Phe Phe Ser Arg Gln EDDnp , as a reference substrate for a systematic specificity study of S 3 to S 3 ' protease subsites ( EDDnp=N [ 2 , 4 dinitrophenyl ] ethylenediamine and Abz=ortho amino benzoic acid ) . ^^^ |
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| Interacting proteins: P29622 and P07339 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29622 and P07339 |
Pubmed |
SVM Score :0.0 |
| NA |
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