Renal tubular absorption of proline, hydroxyproline, and glycine by the newborn of most mammals is inefficient compared to that of the adult. Cortex slices from seven-day-old rat kidney also transport proline and glycine at reduced initial rates compared to mature kidney. Nonetheless, newborn slices achieve higher intracellular concentrations during prolonged incubation; the latter reflects a reduced rate of efflux, a characteristic peculiar to the membrane of postnatal kidney. The postnatal reduction of initial uptake rates is observed clearly only at substrate concentrations in or below the physiological range; it correlates with the absence of two high-affinity systems which normally serve proline and glycine transport independently at these concentrations in mature kidney, in conjunction with a "common" low-affinity system. The low-affinity system alone performs the observed uptake in the newborn kidney. Specific activity of the high-affinity systems for proline and glycine increases asynchronously after birth, suggesting independent genetic control of the three systems for iminoglycine transport in mammalian kidney.

Absorption↗

PubMed1970

Isolation and properties of a beta-alanine transaminaseless mutant of Pseudomonas fluorescens.

beta-Alanine catabolism in Pseudomonas fluorescens is initiated by the enzyme beta-alanine transaminase. We have isolated mutants which fail to produce this enzyme and thus cannot grow on beta-alanine as the sole nitrogen source. The accumulation of beta-alanine-1-(14)C has been studied in one of these mutants, strain 67, and in the wild type. In the mutant, beta-alanine remains in a stable intracellular pool, whereas in the wild type conversion of beta-alanine to an intermediate, presumably malonate semialdehyde, and to CO(2) can be detected. The membrane transport system for beta-alanine can be conveniently studied in this transaminaseless mutant.

Alanine↗

PubMed1970

Neutral amino acid transport in Pseudomonas fluorescens.

Membrane transport of beta-alanine, l-alanine, and l-proline was studied in a beta-alanine transaminaseless mutant (strain 67) of Pseudomonas fluorescens. In this mutant beta-alanine is metabolically inert, and it was therefore possible to demonstrate active transport of this substrate in the absence of intracellular catabolism. The permease which catalyzes the uptake of beta-alanine also transports l-proline and l-alanine. This common transport system was distinguished from permeases which transport only l-alanine and only l-proline by competition studies in strain 67 and by studies of transport specificity in a permeaseless mutant (strain 67/4MTR).

Alanine↗

PubMed1970