Self-quenched fluorogenic protein substrates for the detection of cathepsin D and other protease activities
- 1 February 1989
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 176 (2) , 261-264
- https://doi.org/10.1016/0003-2697(89)90306-0
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivityAnalytical Biochemistry, 1981
- Microcentrifuge desalting: A rapid, quantitative method for desalting small amounts of proteinAnalytical Biochemistry, 1980
- An Intramolecularly Quenched Fluorescent Tripeptide as a Fluorogenic Substrate of Angiotensin‐I‐Converting Enzyme and of Bacterial Dipeptidyl CarboxypeptidaseEuropean Journal of Biochemistry, 1978
- Fluorescence determination of carboxypeptidase A activity based on electronic energy transferAnalytical Biochemistry, 1972
- Use of resonance interaction in the study of the chain folding of insulin in solutionBiochemistry, 1972
- Fluorescein-hemoglobin as a substrate for cathepsin D and other proteasesAnalytical Biochemistry, 1970
- On proteins. CXIII. Specificity of cleavage of heptapeptide substrate with bovine spleen cathepsin DCollection of Czechoslovak Chemical Communications, 1968
- Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide GelsNature, 1962