## Abstract Cathepsin B is a cysteine protease that in tumor tissues is localized in both acidic lysosomes and extracellular spaces. It can catalyze the cleavage of peptide bonds by two mechanisms: endoproteolytic attack with a pH optimum around 7.4, and attack from the __C__βterminus with a pH opt
Biotinylated fluorescent peptide substrates for the sensitive and specific determination of cathepsin D activity
β Scribed by D. Baechle; A. Cansier; R. Fischer; J. Brandenburg; T. Burster; C. Driessen; Dr H. Kalbacher
- Book ID
- 105360420
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 221 KB
- Volume
- 11
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.607
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Several new synthetic substrates fulfilling the specificity requirements of cathepsin D were synthesized. One of these D-Phe-Ser(O-CH2-C6H5)-Phe-Phe-Ala-Ala-pAB(pAB = p-aminobenzoate) proved to be highly sensitive and convenient for measuring activity. Enzyme determination was carried out in a two-s
A method is described for the elucidation of the peptide substrate phosphorylation specificity of a protein kinase. Peptide libraries with two to six degenerate positions and a length of seven or nine amino acids were generated directly on Sepharose beads by solidphase peptide synthesis according to