Zymogen activation as a sensitive enzyme-amplifying assay for a protease with tryptic specificity
| Autor: | Dennis Barrett |
|---|---|
| Rok vydání: | 1970 |
| Předmět: |
History
Embryo Nonmammalian Trypsinogen medicine.medical_treatment Kinetics Education Hydrolysis chemistry.chemical_compound Zymogen medicine Animals Trypsin Enzyme Precursors Protease Chromatography Esters Articles Stimulation Chemical Computer Science Applications Standard curve Biochemistry chemistry Zymogen activation medicine.drug Echinodermata Peptide Hydrolases |
| Zdroj: | The Biochemical journal. 117(1) |
| ISSN: | 0264-6021 |
| Popis: | A protease, ‘trypsinogenase’, secreted in small amounts by the sea-urchin blastula, is assayed in two steps as an example of enzyme-amplifying kinetics. In reaction 1 the trypsinogenase catalyses the activation of trypsinogen to trypsin. In reaction 2 the trypsin catalyses the hydrolysis of N-α-toluene-p-sulphonylarginine methyl ester, at a rate that is linear with trypsinogenase concentration over a 20-fold range. Results are reproducible within a batch of zymogen, but each batch requires a separate standard curve. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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