The reducing terminal of hyaluronate was labeled with a fluorogenic reagent, 2-aminopyridine. The pyridylaminohyaluronate was incubated with testicular hyaluronidase for 1 h. After incubation, 4 vol of ethanol was added to the incubation mixture, followed by centrifugation. The fluorescence of the s
Polyethenoadenosine Phosphate as a Fluorogenic Substrate for Barnase
β Scribed by P.C. Fitzgerald; R.W. Hartley
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 327 KB
- Volume
- 214
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
Polyethenoadenosine phosphate is rapidly hydrolyzed by barnase with an accompanying large increase in fluorescence. At pH 8, 0.2 M ammonium acetate, the initial rate of fluorescence increase is proportional to barnase concentration and thus provides an excellent quantitative assay for its activity. The preparation and use of this substrate in the barnase assay is presented in detail.
π SIMILAR VOLUMES
A fluorogenic substrate for the angiotensin-converting enzyme (EC 3.4.15.1) is presented: para-nitrobenzyloxycarbonylglycyl-~-tryptophylglycine. The assay is based upon relief of the internal quenching of tryptophan fluorescence by the nitrobenzyl group when the substrate is enzymatically hydrolyze
Chromogenic substrates have been generally used in enzymatic assays for the specific determination of heavy metal toxicity. A toxicity assay based on the specific inhibition of β€-galactosidase by heavy metals and using a fluorogenic substrate was evaluated for its sensitivity to heavy metals and org
N,NΠ-Dicyanomethyl-o-phenylenediamine was synthesized with a 90% yield by a reaction of o-phenylenediamine with chloroacetonitrile in triethylamine. Our experimental results showed that it was the effective fluorogenic substrate for horseradish peroxidase (HRP) and hemin. The K m for the HRP system