Molecular specificity of tubular reabsorption of L-proline. A microperfusion study in rat kidney.

In microperfusion experiments the reabsorption of 3H and 14C labelled L-proline by two recently defined transport systems (one with high capacity and low affinity, the other one having the opposite characteristics) was measured in vivo et situ on addition of several amino acids and some N-methylated derivatives. The high capacity system is apparently an unspecific system for neutral amino acids. The methylation of the amino group does not change the affinity to the system. The affinity decreases in the order phenylalanine > glutamine > alanine > proline, hydroxyproline > glycine. The low capacity system seems to be a specific reabsorption mechanism for imino acids like proline, hydroxyproline, sarcosine an N-methylalanine. Common neutral amino acids are not accepted. The different characteristics of both transport systems are also demonstrated by the finding that the affinity of phenylalanine for the high capacity system is about 5 times higher but its affinity for the low capacity system is about 50 times lower than the affinity for proline.