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Merck
CN

Enzyme molecules as nanomotors.

Journal of the American Chemical Society (2013-01-12)
Samudra Sengupta, Krishna K Dey, Hari S Muddana, Tristan Tabouillot, Michael E Ibele, Peter J Butler, Ayusman Sen
摘要

Using fluorescence correlation spectroscopy, we show that the diffusive movements of catalase enzyme molecules increase in the presence of the substrate, hydrogen peroxide, in a concentration-dependent manner. Employing a microfluidic device to generate a substrate concentration gradient, we show that both catalase and urease enzyme molecules spread toward areas of higher substrate concentration, a form of chemotaxis at the molecular scale. Using glucose oxidase and glucose to generate a hydrogen peroxide gradient, we induce the migration of catalase toward glucose oxidase, thereby showing that chemically interconnected enzymes can be drawn together.

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Sigma-Aldrich
葡萄糖氧化酶 来源于黑曲霉, Type X-S, lyophilized powder, 100,000-250,000 units/g solid (without added oxygen)
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葡萄糖氧化酶 来源于黑曲霉, Type VII, lyophilized powder, ≥100,000 units/g solid (without added oxygen)
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尿素酶 来源于洋刀豆 (刀豆), Type III, powder, 15,000-50,000 units/g solid
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尿素酶 来源于洋刀豆 (刀豆), powder, ~1 U/mg
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尿素酶 来源于洋刀豆 (刀豆), powder, white, ~8 U/mg
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