By Mauseth J.D. et al.
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Additional info for A cactus odyssey
1974). Analyses of the two mitochondrial membranes from animal cells (rat liver) show that, in general, they are distinctly different in structure, enzyme content, and lipid composition. Detailed information on the localization of over 50 enzymes on the outer membrane, intermembrane space, inner membrane, and the matrix have been published (ERNSTER and KUYLENSTIERNA, 1970). , 1966; GREEN and PERDUE, 1966; SCHNAITMAN and GREENAWALT, 1968) largely have been resolved (ERNSTER and KUYLENSTIERNA, 1970).
6). Very few integral proteins have been isolated, purified, and characterized, but it is believed that being amphipathic and globular, they possess hydrophobic regions which interact with the lipophilic region in the membrane. This non-polar interaction would then anchor the proteins in the membrane. Proteins so anchored may contain a hydrophilic end extending into the aqueous environment, or in some instances, they appear to contain two polar regions, one on either end. Such molecules could span the membrane and the polar ends would then be exposed to the aqueous environment on either side of the membrane (LENARD and SINGER, 1966; WALLACH and ZAHLER, 1966).
Thus solute transport would involve three phases: (1) solute recognition (solute binding), (2) transmembrane transport (subunit rearrangement), and (3) energy coupling (associated with active transport and accumulation) (SIMONI, 1972; Boos, 1974). SINGER extends this model to include the extrinsic proteins that may be associated with membrane transport. , the periplasmic proteins of gram negative bacteria) bind specific ligands, thus they would be involved in the solute recognition step. Subsequently, it is postulated that they could attach to the hydrophilic ends of specific integral proteins which are at the surface of the membrane.
A cactus odyssey by Mauseth J.D. et al.