Roles of gamma-Globulin in the Dynamic Interfacial Behavior of Mixed Dipalmitoyl Phosphatidylcholine/gamma-Globulin Monolayers at Air/Liquid Interfaces.
This study investigated the roles of gamma-globulin in the dynamic interfacial behavior of dipalmitoyl phosphatidylcholine (DPPC)/gamma-globulin monolayers at air/liquid interfaces at 25 degrees C. The surface tension behavior demonstrated that gamma-globulin had a large adsorption time scale. Moreover, the surface pressure-area hysteresis behavior of adsorbed gamma-globulin monolayers suggested that no significant desorption occurred during the compression stage, and the respreading of gamma-globulin molecules at the interface during the expansion stage was slow. From the hysteresis behavior of adsorbed gamma-globulin monolayers with spread DPPC molecules, it was found that gamma-globulin molecules were expelled from the interface as DPPC molecules were in a condensed state. The squeeze-out of gamma-globulin molecules seemed to induce the loss of DPPC molecules at the interface with the extent depending on the initial gamma-globulin surface concentration. Furthermore, the expelled gamma-globulin molecules re-entered the monolayer and participated in the surface pressure increase during the following expansion stage. The exclusion of gamma-globulin associated with the removal of DPPC during monolayer compression and the re-entry of gamma-globulin during subsequent monolayer expansion represented a mechanism for DPPC depletion and gamma-globulin enrichment at the interface, which may explain the inhibitory effect of certain proteins on the surface activity of DPPC. Copyright 2000 Academic Press.
Chang
CH
Department of Chemical Engineering, National Cheng Kung University, Tainan, 70101, Taiwan, Republic of China
Yu
SD
Chuang
TK
Liang
CN