Incorporation of D-glucose-, L-alanine- and phosphate-transport systems from rat renal brush-border membranes into liposomes.
An extract of soluble proteins was prepared from a rat kidney brush-border membranes by Triton X-100 solubilization followed by centrifugation for 1 h at 100000g. Its protein composition was markedly different from that of the brush-border membranes. Proteoliposomes were formed by co-sonication of the Triton X-100-free extract with a naturally occurring mixture of phospholipids extracted from rat kidney. These proteoliposomes were shown to contain Na+-stimulated D-glucose-, L-alanine- and phosphate-transport systems.
D000409:Alanine / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D004591:Electrophoresis, Polyacrylamide Gel; D005947:Glucose / Q000378:metabolism; D007672:Kidney Cortex / Q000378:metabolism*; D008081:Liposomes; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D008871:Microvilli / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D011092:Polyethylene Glycols; D051381:Rats
D008081:Liposomes; D008565:Membrane Proteins; D010710:Phosphates; D011092:Polyethylene Glycols; D005947:Glucose; D000409:Alanine