Transport of imino acids and non-α-amino acids across the brush-border membrane of the rabbit ileum

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Abstract
The transport of β-alanine and MeAIB and their effects as inhibitors of the transport of alanine, leucine and lysine across the brush-border membrane of the intact epithelium from the rabbit's distal ileum has been examined. Two separate transport systems have been characterized: 1) A sodium-dependent, β-alanine-accepting system, which is a high-affinity transport system for α-amino-monocarboxylic acids (neutral a.a.) and for cationic a.a., accepts non-α-amino acids as well as non-α-imino acids, is moderately stereospecific, and for which the affinity of a neutral a.a. is greatly reduced by N-methylation. 2) A sodium-dependent transport system for imino acids, which is inaccessible to cationic amino acids and non-α-amino acids but accepts cyclic, non-α-imino acids, is moderately stereospecific, and for which neutral a.a. have much lower affinities than their N-methylated derivatives. On the basis of the observations of this and the preceding paper five transport systems for amino acids are ascribed to the rabbit ileum. Some discrepancies between the present results and those obtained with brush-border membrane microvesicles from the rabbit small intestine are discussed.