Realflight Dongle Emulator 3.4.18

Version" description="0x10 Subsystem Device" aliases="0x10 Subsystem Device" groups="0x0 Emulation Plugins" vendor="0x10 (Ralflight Dongle Emulator)">

Substrate recognition and binding in porin/concanavalin A and concanavalin A/P1A complexes.

The binding of concanavalin A to liposomes was studied by means of steady-state and time-resolved fluorescence measurements. A simplified explanation of the results of the steady-state measurements is that the binding of concanavalin A to liposomes occurs at two different sites: at low concanavalin A concentrations the binding is by a conventional interaction, while at high concanavalin A concentrations the binding is by a non-cooperative aggregation of concanavalin A, without an associated change in fluorescence. At high concanavalin A concentrations a further change in fluorescence intensity was observed upon dilution of the solution, indicating that some aggregation took place in the course of the time-resolved measurements. The results of the time-resolved measurements are consistent with the two-site model of binding, but suggest that the rate of conformational change to the aggregated state is very rapid, less than 10(-9) s-1. The specific binding of concanavalin A to porin was also studied by means of steady-state and time-resolved fluorescence. The binding was concentration dependent, with saturable binding sites. The time-resolved measurements also indicated a two-site model of binding, in which binding was accompanied by a conform 0b46394aab

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