Plasma membranes structure

Laisson C, Moller IM. The Plant Plasma Membrane Structure, Function and Molecular Biology, Springer-Verlag, New York, 1990. 

For more details of plasma membrane structure, see the section Bibliography. 7... 

Antibacterial agents which act on the plasma membrane structure 195... 

Mahadik, S.P., Bharucha, V.A., Stadlin, A., Ortiz, A, and Karpiak, S.E. (1992) Loss and recovery of activities of al-pha and alpha isoenzymes of (Na" " + K )-ATPase in cortical focal ischemia GMl ganglioside protects plasma membrane structure and function. J. Neurosci. Res. 32 209-220. 

It is the post-pulse state that is relevant of most effects dealing with delivery. Its structural organization remains unclear. Electropermeabilization alters cell plasma membrane structure. 

Prokaryotic cells have only a single membrane, the plasma membrane or cell membrane. Because they have no other membranes, prokaryotic cells contain no nucleus or organelles. Nevertheless, they possess a distinct nuclear area where a single circular chromosome is localized, and some have an internal membranous structure called a mesosome that is derived from and continuous with the cell membrane. Reactions of cellular respiration are localized on these membranes. In photosynthetic prokaryotes such as the cyanobacteria,... 

FIGURE 10.18 A model for the structure of the a-factor transport protein in the yeast plasma membrane. Gene duplication has yielded a protein with two identical halves, each half containing six transmembrane helical segments and an ATP-binding site. Like the yeast a-factor transporter, the multidrug transporter is postulated to have 12 transmembrane helices and 2 ATP-binding sites. 

Most ABC-transporters, especially those located in the plasma membrane, are phosphorylated and glycosylated transmembrane proteins of different molecular weights (e.g., P-gp 170 kDa MRP2 190 kDa BCRP 72 kDa). Topologically, most ABC-transporter show a similar structure they are organized in two transmembrane domains (TMD), each consisting of six... 

C1C-6 and C1C-7 define the third branch of the CLC family. These proteins are only about 45% identical to each other. Whereas CLC-7 is very broadly expressed, the CLC-6 protein seems to be restricted to the nervous system. It proved impossible to obtain plasma membrane chloride currents with either C1C-6 or C1C-7. This is due to the fact that both channels reside in intracellular organelles under most circumstances. Based on structural features, it appeals likely that they also mediate CF/H + exchange. 

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