Structure, composition, enzymatic activities of human erythrocyte and sarcoplasmic reticulum membrane films.
Air/water interface films were obtained from human erythrocytes and rabbit sarcoplasmic reticulum membranes at 'zero surface pressure. according to Verger, R and Pattus, F. (Chem. Phys. Lipids (1976) 16, 285-291). The lipid and protein distribution of these membrane films suggest that the film composition is determined by the composition of the membrane and the mode of integration of its components. When kept at low surface pressure, slow film expansion occurred due to unfolding of proteins at the interface. This process can be stopped by compressing the films at a higher surface pressure than 15 dyn/cm. Acetylcholinesterase activity from human erythrocyte films is highly dependent on the condensation state of the film. Ca2+-ATPase from sarcoplasmic reticulum films was still activable by Ca2+. Freeze-fracture studies on erythrocyte membrane films suggest the such films are monolayers in which proteins are randomly distributed.
D000110:Acetylcholinesterase / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000032:analysis*; D004912:Erythrocytes / Q000032:analysis*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008563:Membrane Lipids / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D008854:Microscopy, Electron; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000032:analysis*; D013499:Surface Properties; D013552:Swine
D008563:Membrane Lipids; D008565:Membrane Proteins; D000255:Adenosine Triphosphate; D000110:Acetylcholinesterase; D000252:Calcium-Transporting ATPases