Transport of neutral and cationic amino acids across the brush-border membrane of the rabbit ileum.

Abstract

The transport of sugars and amino acids across the brush-border membrane of the distal rabbit ileum has been studied. The kinetics of the transport of glucose demonstrated that the data obtained with the present technique are less distorted by unstirred layers than those obtained with the same technique adapted to the use of magnetic stirring. The role of depolarization of the electrical potential difference across the brush-border membrane in mutual inhibition between different classes of amino acids was estimated by measurements of the effects of high concentrations of alanine and lysine on the transport of galactose. It was found that this role would be insignificant in the present study. By measurements of the transport of alanine, leucine and lysine and the inhibitory interactions between these amino acids the function of three transport systems has been delineated. The transport of lysine is resolved in a high- and a low-affinity contribution. At 140 mM sodium these transport systems may also function as respectively high- and low-affinity contributors to the transport of neutral amino acids. At 0 mM sodium the high-affinity system remains a high-affinity system for cationic and neutral amino acids with reduced capacity especially for the neutral amino acids. At 0 mM sodium the low-affinity system's affinity for lysine is reduced and it is inaccessible to neutral amino acids. In addition to the two systems for lysine transport the existence of a lysine-resistant, sodium-dependent, high-affinity system for the transport of neutral amino acids has been confirmed. It seems unlikely that the distal ileum is equipped with a low-affinity, sodium-independent system for the transport of neutral amino acids.