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- W1978312035 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 ..." @default.
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- W1978312035 date "1989-07-01" @default.
- W1978312035 modified "2023-09-23" @default.
- W1978312035 title "Thermotropic Behavior of Proteins and Acylated Proteins in Monolayers" @default.
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- W1978312035 doi "https://doi.org/10.1246/bcsj.62.2299" @default.
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