A direct spectrophotometric assay for d-alanine carboxypeptidases and for the esterase activity of β-lactamases
✍ Scribed by R.F. Pratt; W.Stephen Faraci; Chandrika P. Govardhan
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 258 KB
- Volume
- 144
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A direct spectrophotometric pH indicator method has been devised to assay the activity of the D-Ala carboxypeptidase/transpeptidase of Streptomyces R61, and which should be of general application to D-Ala carboxypeptidases. The substrate employed is N,N'diacetyl-r.lysyl-D-alanyl-D-lactate. The method allows the determination of steady-state kinetic parameters, and can also be used for the assay of the esterase activity of Blactamases against specific depsipeptides. 0 1985 Academic prss. Inc.
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We developed a specific spectrophotometric assay for the quantitative determination of phospholipase D-catalyzed transphosphatidylation activity. The assay measures p-nitrophenol liberated by phospholipase D-catalyzed reaction of phosphatidyl-p-nitrophenol and ethanol in an aqueous-organic emulsion