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• W2068751752 abstract "The behavior of the enzyme acetylcholinesterase was studied at the air/water interface. Surface pressure–area (π–A) isotherms and UV–vis spectra recorded at different surface pressures were determined for different salt concentrations in the subphase. The ionic strength of the subphase does not influence the physical properties in consideration; however, the pH of the subphase has a great effect on its surface and optical properties. A subphase at pH 6.5 has shown that the enzyme is highly stable, based on the π–Acompression/decompression isotherms. No changes in the area per molecule were observed when the surface pressure was maintained constant at 16 mN/m for a period of 120 min. The long-term stability of acetylcholinesterase at the air/water interface was demonstrated for pH 6.5 and a salt concentration of 10−2M(KCl). The absorption spectra of the monolayer, measured directly at the air/water interface, are considered good evidence of the organization of the enzyme molecules." @default.
• W2068751752 created "2016-06-24" @default.
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• W2068751752 date "1997-10-01" @default.
• W2068751752 modified "2023-09-27" @default.
• W2068751752 title "Surface and Spectroscopic Properties of Acetylcholinesterase Monolayer at the Air/Water Interface" @default.
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• W2068751752 doi "https://doi.org/10.1006/jcis.1997.5069" @default.
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