Surface behavior of myelin monolayers.

RAFAEL GUSTAVO OLIVEIRA; CALDERÓN, R. O.; MAGGIO, B.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

ELSEVIER SCIENCE BV

Año: 1998 vol. 1370 p. 127 - 127

0005-2736

yelin can be spread as a stable monomolecular layer, with reproducible properties, at the air?water interface. The major lipids and proteins of myelin are represented in this monolayer in molar ratios similar to those in the original membrane. A well-defined collapse point of the myelin monolayer occurs at ca. 46mNrm. At a surface pressure of ca. 20mNrm, the surface pressure?molecular area isotherm of the myelin monolayer shows a change in its compressibility,exhibited as a diffuse but reproducible inflection with a clearly marked change of the surface compressional modulus; the surface potential?area curve shows a change of slope at the same surface pressure. The myelin monolayer shows considerable hysteresis during the first compression?decompression cycle; no detectable protein unfolding under expansion; and decreased hysteresis after the first cycle. The average molecular areas, the inflection at 20mNrm, the variation of the surface potential per unit of molecular surface de