Julia M. La Nauze

TL;DR: Phosphonatase is inhibited by CN−, S2− and SO32−, which suggests that disulphide bridges may be necessary in maintaining the tertiary structure of the activeform of the enzyme.

TL;DR: Kinetic experiments showed that the transport system has a high affinity for aminoethylphosphonic acid and that ther transport process itself is not inhibited by orthophosphate or Orthophosphite, although the latter prevents the further utilization of the substrate.

TL;DR: The primary pool appears to be closely related to the external phosphate and to its transport, since it does not interact with phosphate liberated within the cell from α-glycerophosphate, and isotope displacement experiments show that phosphate, taken up from that point in time, still passes through that pool.

TL;DR: Support for the hypothesis that all four anions might share a common component of a transport syste was provided by the demonstration of counter-exchange diffusion between orthophosphate and arsenate, and from kinetics studies of the competitive inhibition by orthoph phosphite of the uptake of Orthophosphite and arsenates.