EC 3.1.1.14) was isolated and purified from Phaseolus vulgaris L. chloroplasts and etioplasts dissolved in 1% Triton X-100 and 10% glycerol. A 100 and 40-fold purification, respectively, was achieved. Enzyme preparations from both sources had similar affinities for chlorophyll a when assayed in a T
Triton X-100 reacts with chlorophyll in the presence of chlorophyllase
β Scribed by T.J. Michalski; C. Bradshaw; J.E. Hunt; J.R. Norris; J.J. Katz
- Book ID
- 115919409
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 403 KB
- Volume
- 226
- Category
- Article
- ISSN
- 0014-5793
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π SIMILAR VOLUMES
The Lowry procedure has been modified for use in the presence of Triton X-100 (TX-loo) by the addition of 10% sodium dodecyl sulfate. The method is applicable to samples containing 40-120 pg protein.
During our studies of the polynucleotide phosphorylase of rat liver mitochondrial membranes (1,2), we have needed to assay phosphatase, pyrophosphatase, and nucleoside diphosphatase activities in the presence of Triton X-100 used (2) to solubilize the membrane-bound polynucleotide phosphorylase. The
In a pH 7.0 buffer solution containing 0.0020% Triton X-100 CPZ yields a sensitive polarographic wave at -1.90 V, which can be used to determine trace amounts of the drug, the detection limit being 4.2 Γ 10 -9 mol/liter. Using potentiostatic coulometry, chronocoulometry, and cyclic voltammetry the e