Transport of 14C-L-glycine by the haustorial mycoparasite Tieghemiomyces parasiticus in axenic culture.
Transport of L-glycine by the haustorial mycoparasite Tieghemiomyces parasiticus grown in axenic culture was investigated using endogenously metabolizing cells. Transport occurred against a concentration gradient and required the expenditure of energy supplied by metabolic reactions that were inhibited by catalytic amounts of sodium azide and 2,4-dinitrophenol. The process exhibited both pH and temperature dependence with optima at pH 4 and 35 degrees C, respectively. The energy of activation and Q10 for transport were calculated to be 18,227 cal/mole and 2.82 respectively, between 20 and 30 degrees C. The kinetics of the system were consistent with a mechanism of transport that depended upon a finite number of sites on the cell surface and had a Kt of 1.46 x 10(-5) M. The system for L-glycine transport lacked sterospecificity and was most inhibited in the presence of other neutral amino acids while less inhibition was observed in the presence of the acidic and basic amino acids. These results suggest that L-glycine transport in this mycoparasite occurs by an energy dependent, protein-mediated process characteristic of active transport.
Transport of 14C-L-glycine by the haustorial mycoparasite Tieghemiomyces parasiticus in axenic culture. Transport of L-glycine by the haustorial mycoparasite Tieghemiomyces parasiticus grown in axenic culture was investigated using endogenously metabolizing cells. Transport occurred against a concentration gradient and required the expenditure of energy supplied by metabolic reactions that were inhibited by catalytic amounts of sodium azide and 2,4-dinitrophenol. The process exhibited both pH and temperature dependence with optima at pH 4 and 35 degrees C, respectively. The energy of activation and Q10 for transport were calculated to be 18,227 cal/mole and 2.82 respectively, between 20 and 30 degrees C. The kinetics of the system were consistent with a mechanism of transport that depended upon a finite number of sites on the cell surface and had a Kt of 1.46 x 10(-5) M. The system for L-glycine transport lacked sterospecificity and was most inhibited in the presence of other neutral amino acids while less inhibition was observed in the presence of the acidic and basic amino acids. These results suggest that L-glycine transport in this mycoparasite occurs by an energy dependent, protein-mediated process characteristic of active transport.