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A fluorometric method for the determination of the tryptophan content of proteins

✍ Scribed by T. Sasaki; B. Abrams; B.L. Horecker

Publisher
Elsevier Science
Year
1975
Tongue
English
Weight
526 KB
Volume
65
Category
Article
ISSN
0003-2697

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✦ Synopsis

Digestion of proteins with a mixture of chymotrypsin and pronase followed by dilution in 6 M urea eliminates the quenching effects usually observed when tryptophan fluorescence is measured in native or denatured proteins. Following proteolysis, the tryptophan content can be estimated from the fluorescence emission, using free tryptophan as an internal standard. The values obtained for a number of proteins are in agreement with the literature values. The method can be applied to as little as 40 pg of protein sample.

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A rapid and sensitive fluorometric assay for the measurement of carnitine palmitoyltransferase (CPT) activity is described. In this assay the coenzyme A (CoA) liberated from palmitoyl-CoA by CPT reacts with N-(9-acridinyl)-maleimide to form a fluorescent product. By comparing the fluorescence intens