Complexation nonspecific surface

The overall distribution of lanthanides in bone may be influenced by the reactions between trivalent cations and bone surfaces. Bone surfaces accumulate many poorly utilized or excreted cations present in the circulation. The mechanisms of accumulation in bone may include reactions with bone mineral such as adsorption, ion exchange, and ionic bond formation (Neuman and Neuman, 1958) as well as the formation of complexes with proteins or other organic bone constituents (Taylor, 1972). The uptake of lanthanides and actinides by bone mineral appears to be independent of the ionic radius. Taylor et al. (1971) have shown that the in vitro uptakes on powdered bone ash of 241Am(III) (ionic radius 0.98 A) and of 239Pu(IV) (ionic radius 0.90 A) were 0.97 0.016 and 0.98 0.007, respectively. In vitro experiments by Foreman (1962) suggested that Pu(IV) accumulated on powdered bone or bone ash by adsorption, a relatively nonspecific reaction. On the other hand, reactions with organic bone constituents appear to depend on ionic radius. The complexes of the smaller Pu(IV) ion and any of the organic bone constituents tested thus far were more stable (as determined by gel filtration) than the complexes with Am(III) or Cm(III) (Taylor, 1972). 

As seen above (equation (5)), the basis of the simple bioaccumulation models is that the metal forms a complex with a carrier or channel protein at the surface of the biological membrane prior to internalisation. In the case of trace metals, it is extremely difficult to determine thermodynamic stability or kinetic rate constants for the adsorption, since for living cells it is nearly impossible to experimentally isolate adsorption to the membrane internalisation sites (equation (3)) from the other processes occurring simultaneously (e.g. mass transport complexation adsorption to other nonspecific sites, Seen, (equation (31)) internalisation). 

Moreover, the unique adsorption properties of GEC allowed the very sensitive electrochemical detection of DNA based on its intrinsic oxidation signal that was shown to be strongly dependent of the multi-site attachment of DNA and the proximity of G residues to GEC [100]. The thick layer of DNA adsorbed on GEC was more accessible for hybridization than those in nylon membranes obtained with genosensors based on nylon/GEC with a changeable membrane [99,101,102]. Allhough GEC has a rough surface, it is impermeable, while nylon is more porous and permeable. DNA assays made on an impermeable support are less complex from a theoretical standpoint [7] the kinetics of the interactions are not compUcated by the diffusion of solvent and solutes into and out of pores or by multiple interactions that can occur once the DNA has entered a pore. This explained the lower hybridization time, the low nonspecific adsorplion and the low quantity of DNA adsorbed onto GEC compared to nylon membranes. 

Abstract The immobilization of nucleic acids onto substrates in array fabrication is a complex process involving three major steps (i) the chemical modification of the arrayed material in such a fashion that it can interact with complementary functionalities present on the substrate to form a stable bond (ii) the coating of the support surface with adequate fimctional groups to allow specific binding and prevent nonspecific adsorption of the material to be arrayed and (iii) the use of a delivery system that brings small quantities of the arrayed material to specific positions on the surface. 

The role of lecithin as an auxiliary lipid in the specific interaction of lactosides with globulin in monolayers is related to two processes complex formation between 3 or 4 molecules of lactoside and each lecithin molecule, and the protection of the lactoside molecules in surface micelles from nonspecific interaction. The location of lecithin at the periphery of the surface micelle would explain why the mixed micelle behaves as lecithin in nonspecific interaction. Lactoside molecules, located in the center of the surface micelle, would be in a position to interact specifically with antibody in the aqueous subphase (5). 

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