## Abstract The present work describes the selective covalent modification of fructose bisphosphate aldolase in crude extracts of chicken breast muscle by fluorescein 5′‐isothiocyanate (5′‐FITC) at pH 7.0 and 35°C. The modification was observed after 1 min while no other major soluble protein was l
Continuous colorimetric monitoring of the fructose bisphosphate aldolase reaction
✍ Scribed by Philmore Robertson Jr.; Irwin Fridovich
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 223 KB
- Volume
- 108
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
A simple method for continuous spectrophotometric assay of fructose-1,6-bisphosphate aldolase is described. The method is based on the reactivity of the product triose phosphates with cyanide to form compounds capable of the reduction of cytochrome c. At the concentrations employed, cyanide, acting catalytically, reacts with the enediol tautomer of the triose phosphates to generate the reductants, which reduce cytochrome c causing increased absorbance at 550 nm. The rate of increase in the rate of appearance of SO-nm absorbance is directly proportional to the concentration of aldolase present. The procedure is particularly useful for Class I aldolases, since the assay must be run under mildly alkaline conditions.
📜 SIMILAR VOLUMES