Sensitive and reproducible assay method for chymotrypsin
โ Scribed by B. L. Kabacoff; M. Umhey; A. Wohlman; S. Avakian
- Publisher
- John Wiley and Sons
- Year
- 1963
- Tongue
- English
- Weight
- 338 KB
- Volume
- 52
- Category
- Article
- ISSN
- 0022-3549
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๐ SIMILAR VOLUMES
Sensitive fluorogenic substrates for trypsin, chymotrypsin, and elastase were prepared. These substrates are amides of an acyl amino acid or peptide with 7-amino-4-methyicoumarin (AMC). The substrates with their respective K,,,/K, ratios given in parentheses are: for chymotrypsin, glutaryl-Phe-AMC (
A simplified assay method is described for the determination of protein kinase activity. Enzymatic activity is followed by measuring the incorporation of 32P from the terminal phosphoryl group of nucleoside triphosphates into protein substrate. Separation of the resulting 32P-labeled phosphoprotein
A spectrophotometric method for the assay of hyaluronidase activity, based on the binding of a carbocyanine dye (l-ethyl-2-[3-( l-ethyl-naphtho[l,M] to undegraded substrate, is described. The binding results in a spectral shift with an absorbance maximum at 640 nm which is propo~ional to the amount
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