Abstract
Abstract In order to obtain information concerning the effect of proteins on the thermotropic properties of biological membranes, the temperature-dependences of monolayers of different proteins and some acyl derivatives of bovine serum albumin (BSA) have been investigated. The hydrophobic proteins such as hemoglobin, β-lactoglobulin, and β-casein formed dilute monolayers, whereas the hydrophilic proteins such as cytochrome C and lysozyme formed concentrated monolayers. BSA showed an intermediate isotherm between those of dilute and concentrated films. The monolayers of BSA, cytochrome C, and lysozyme were gradually expanded with increasing temperatures. However, the temperature-dependences of the monolayers of hemoglobin, β-lactoglobulin, β-casein, and acyl derivatives were significantly different from those of the monolayers of hydrophilic proteins. In detail, the monolayers of hemoglobin and β-lactoglobulin formed the most compact structures around 20 °C and 30 °C, respectively, while the monolayers of β-casein formed the most expanded structure around 30 °C. In addition, the monolayers of acetyl and propionyl derivatives formed the most compact structures around 30 °C. These results suggest that the hydrophobicity of protein is an important factor relating to thermal stability of proteins in monolayers.
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