[Interaction of leucine with the plasma membranes of catfish taste buds].
The binding of L-[3H]leucine by the plasma membranes from the catfish Ictalurus nebulosus taste organ was studied. The two types of specific binding centers for amino acid with high (KD = 2,5 X 10(-10) M) and low (KD = 1,04 X 10(-9) M) affinities were found. Concentrations of high and low affinity centers were 11,85 nmol/mg and 26 nmol/mg respectively. The structural rearrangement of the surface layer of the chemoreceptor membrane was revealed by spin label technique using 5-doxylstearic acid at leucine concentrations 10(-4)-10(-9) M.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D005399:Fishes / Q000502:physiology*; D007700:Kinetics; D007930:Leucine / Q000378:metabolism*; D009708:Nucleotidases / Q000378:metabolism; D013650:Taste Buds / Q000378:metabolism* / Q000648:ultrastructure
D009708:Nucleotidases; D007930:Leucine
Vzaimodeĭstvie leĭtsina s plazmaticheskimi membranami vkusovykh lukovits karlikovogo somika.