Purification of cardiolipin for surface pressure studies.

Houle, André; Téchy, F.; Aghion, Jacques; Leblanc, Roger M.

doi:10.1016/s0022-2275(20)38148-7

Cited by 9 publications

(1 citation statement)

References 17 publications

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“…The lattice constants are much greater than the intermolecular distance of a closely packed CL layer, which indicates that we cannot simply interpret each blob in the filtered image as a single CL molecule. This conclusion is supported by the fact that the surface area, determined from the surface pressure versus molecular area isotherms (Figure ), is an order of magnitude smaller than the area of a unit cell in the AFM image. The periodic structure with such large lattice constants must be due to the fact that the individual CL molecules organize themselves into a higher order structure which, unfortunately, cannot be determined based on the present images.…”

Section: Resultsmentioning

confidence: 80%

Electron-Transfer Properties of Cytochrome c Langmuir−Blodgett Films and Interactions of Cytochrome c with Lipids

et al. 1998

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The structural and electron-transfer properties of cytochrome c (Cyt c) Langmuir−Blodgett (LB) films have been studied on graphite electrode with tapping mode atomic force microscopy and cyclic voltammetry (CV). Cyt c in the LB films forms an ordered monolayer in which the individual proteins pack into a quasi-hexagonal structure. The monolayer undergoes a reversible electron-transfer reaction in phosphate buffer. The interactions of Cyt c with cardiolipin (CL) and phosphatidylcholine (PC) LB films have been studied. The LB films of CL and PC are both ordered on graphite, but their interactions with Cyt c are quite different. On a CL monolayer, Cyt c adsorbs spontaneously and the adsorbed protein preserves the electron-transfer reaction. However, on a PC monolayer, Cyt c does not adsorb.

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Section: Resultsmentioning

confidence: 80%