Activation of acetylcholinesterase by Triton X-100
β Scribed by R. Srinivasan; A. Karczmar; J. Bernsohn
- Book ID
- 115732790
- Publisher
- Elsevier Science
- Year
- 1972
- Weight
- 408 KB
- Volume
- 284
- Category
- Article
- ISSN
- 0005-2744
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π SIMILAR VOLUMES
A simple permeabilization procedure has been developed which allows the reliable determination of enzyme activities in situ in a variety of different microorganisms. Permeabilization is obtained by freezing cell suspensions in the presence of a low concentration of the anionic detergent Triton X-100
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