Substrate solubilization for the Hummel α-chymotrypsin assay
✍ Scribed by K.N. Rao; Benito Lombardi
- Book ID
- 107711750
- Publisher
- Elsevier Science
- Year
- 1975
- Tongue
- English
- Weight
- 222 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A well-known and often-used assay for the determination of esterolytic activity of chymotrypsin is the Hummel method (1). It is based on the rate of hydrolysis of N-benzoyl-n-tyrosine ethyl est'er (BTEE) as determined by the change in absorbancy at 256 nm. The assay is the first choice of many labor
The use o f 6-(N-acetyl-~-phenylalanyl)-aminoluciferin as a novel substrate for achymotrypsin has been demonstrated. The kinetic parameters determined are K M = 0.38 mmol/L, kcat = 6.5 s-' and kcat/kM = 17,100 (L/mol s). The test principle o f the coupled assay is the release o f aminoluciferin by e