Molecular sizes of amino acid transporters in the luminal membrane from the kidney cortex, estimated by the radiation-inactivation method
- 15 May 1990
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 268 (1), 195-200
- https://doi.org/10.1042/bj2680195
Abstract
Renal brush-border membrane vesicles from rat kidney cortex were irradiated in frozen state with a gamma-radiation source. Initial rates of influx into these vesicles were estimated for substrates such as L-glutamic acid, L-alanine, L-proline and L-leucine to establish the molecular sizes of their carriers. Transport was measured in initial-rate conditions to avoid artifacts arising from a decrease in the driving force caused by a modification of membrane permeability. Initial rates of Na(+)-independent uptakes for those four substrates appeared unaffected in the dose range used (0-6 Mrad), indicating that the passive permeability of the membrane towards these substrates was unaffected. However, at higher doses of irradiation the Na+ influx and the intravesicular volume evaluated by the uptake of glucose at equilibrium were altered by radiation. Thus Na(+)-dependent influx values were corrected for volume changes, and the corrected values were used to compute radiation-inactivation sizes of the transport systems. Their respective values for L-glutamic acid, L-proline, L-leucine and L-alanine carriers were 250, 224, 293 and 274 kDa. The presence of the free-radicals scavenger benzoic acid in the frozen samples during irradiation did not affect the uptake of glucose, phosphate and alkaline phosphatase activity. These results indicate that freezing samples in a cryoprotective medium was enough to prevent secondary inactivation of transporters by free radicals. Uptakes of beta-alanine and L-lysine were much less affected by radiation. The radiation-inactivation size of the Na(+)-dependent beta-alanine carrier was 127 kDa and that of the L-lysine carrier was 90 kDa.This publication has 19 references indexed in Scilit:
- Molecular size of the Na+-H+ antiport in renal brush border membranes, as estimated by radiation inactivationBiochemical and Biophysical Research Communications, 1988
- Mechanisms of Transport of Amino Acids Across MembranesAnnual Review of Nutrition, 1987
- Evidence for a single common Na+-dependent transport system for alanine, glutamine, leucine and phenylalanine in brush-border membrane vesicles from bovine kidneyBiochimica et Biophysica Acta (BBA) - Biomembranes, 1987
- On the strategy of kinetic discrimination of amino acid transport systemsThe Journal of Membrane Biology, 1985
- Factors affecting the transport of β-amino acids in rat renal brush-border membrane vesicles. The role of external chlorideBiochimica et Biophysica Acta (BBA) - Biomembranes, 1985
- Organic ion transport during seven decades the amino acidsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1984
- Proton-coupledl-lysine uptake by renal brush border membrane vesicles from mullet (Mugil cephalus)The Journal of Membrane Biology, 1983
- Delineation of sodium-stimulated amino acid transport pathways in rabbit kidney brush border vesiclesThe Journal of Membrane Biology, 1982
- Phenylalanine uptake in isolated renal brush border vesiclesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1976
- Membrane enzyme systems molecular size determinations by radiation inactivationBiochimica et Biophysica Acta (BBA) - Biomembranes, 1968