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  • Title: L-lysine transport in chicken jejunal brush border membrane vesicles.
    Author: Torras-Llort M, Ferrer R, Soriano-García JF, Moretó M.
    Journal: J Membr Biol; 1996 Aug; 152(3):183-93. PubMed ID: 8672084.
    Abstract:
    The properties of l-lysine transport in chicken jejunum have been studied in brush border membrane vesicles isolated from 6-wk-old birds. l-lysine uptake was found to occur within an osmotically active space with significant binding to the membrane. The vesicles can accumulate l-lysine against a concentration gradient, by a membrane potential-sensitive mechanism. The kinetics of l-lysine transport were described by two saturable processes: first, a high affinity-transport system (KmA = 2.4 +/- 0.7 micromol/L) which recognizes cationic and also neutral amino acids with similar affinity in the presence or absence of Na+ (l-methionine inhibition constant KiA, NaSCN = 21.0 +/- 8.7 micromol/L and KSCN = 55.0 +/- 8. 4 micromol/L); second, a low-affinity transport mechanism (KmB = 164. 0 +/- 13.0 micromol/L) which also recognizes neutral amino acids. This latter system shows a higher affinity in the presence of Na+ (KiB for L-methionine, NaSCN = 1.7 +/- 0.3 and KSCN = 3.4 +/- 0.9 mmol/L). L-lysine influx was significantly reduced with N-ethylmaleimide (0.5 mmol/L) treatment. Accelerative exchange of extravesicular labeled l-lysine was demonstrated in vesicles preloaded with 1 mmol/L l-lysine, l-arginine or l-methionine. Results support the view that l-lysine is transported in the chicken jejunum by two transport systems, A and B, with properties similar to those described for systems b0,+ and y+, respectively.
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