Sheĭko L M, Ostretsova I B, Levko A V, Volotovskiĭ I D, Etingof R N
Mol Biol (Mosk). 1983 Nov-Dec;17(6):1220-6.
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.
对鲶鱼(Ictalurus nebulosus)味觉器官的质膜结合L-[3H]亮氨酸的情况进行了研究。发现了两种对氨基酸具有高亲和力(KD = 2.5×10⁻¹⁰ M)和低亲和力(KD = 1.04×10⁻⁹ M)的特异性结合中心。高亲和力中心和低亲和力中心的浓度分别为11.85 nmol/mg和26 nmol/mg。使用5-硬脂酰氧基氮氧自由基,在亮氨酸浓度为10⁻⁴ - 10⁻⁹ M的条件下,通过自旋标记技术揭示了化学感受器膜表层的结构重排。