| Literature DB >> 18280491 |
Luciano Caseli1, Douglas C Masui, Rosa P M Furriel, Francisco A Leone, Maria E D Zaniquelli, Jhony Orbulescu, Roger M Leblanc.
Abstract
A glycosylphosphatidylinositol (GPI)-anchored enzyme (rat osseous plate alkaline phosphatase-OAP) was studied as monolayer (pure and mixed with lipids) at the air-water interface. Surface pressure and surface potential-area isotherms showed that the enzyme forms a stable monolayer and exhibits a liquid-expanded state even at surface pressure as high as 30 mN m(-1). Isotherms for mixed dimyristoylphosphatidic acid (DMPA)-OAP monolayer showed the absence of a liquid-expanded/liquid-condensed phase transition as observed for pure DMPA monolayer. In both cases, pure or mixed monolayer, the enzyme preserves its native conformation under compression at the air-water interface as observed from in situ p-polarized light Fourier transform-infrared reflection-absorption spectroscopic (FT-IRRAS) measurements. Changes in orientation and conformation of the enzyme due to the presence or absence of DMPA, as well as due to the surface compression, are discussed.Entities:
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Year: 2008 PMID： 18280491 DOI： 10.1016/j.jcis.2008.01.043
Source DB: PubMed Journal: J Colloid Interface Sci ISSN： 0021-9797 Impact factor: 8.128