Baldwin J M, Bennett J P, Gomperts B D
Eur J Biochem. 1983 Oct 3;135(3):515-8. doi: 10.1111/j.1432-1033.1983.tb07682.x.
Digitonin was found to be the only detergent (out of 24 tested) capable of solubilising the chemotactic formyl peptide receptor from rabbit neutrophil membranes in a form which retained its [3H]fMet-Leu-Phe binding activity. The solubilised material retained many of the characteristics of the membrane-bound receptor. [3H]fMet-Leu-Phe binding to the digitonin extract was measured at 4 degrees C using an equilibrium dialysis assay. Binding was saturable and of high affinity (Kd = 3.5 +/- 0.7 nM). The potencies of a series of synthetic peptides as inhibitors of [3H]fMet-Leu-Phe binding to the soluble receptor showed the same rank order as for inhibition of the membrane-bound receptor. In addition, binding to both preparations was sulphydryl dependent showing a parallel inhibition by p-chloromercuribenzene sulphonate which could be partially reversed by subsequent incubation with dithiothreitol.
洋地黄皂苷是唯一一种（在测试的24种洗涤剂中）能以保留其[3H]甲硫氨酰-亮氨酰-苯丙氨酸结合活性的形式溶解兔中性粒细胞膜上趋化性甲酰肽受体的洗涤剂。溶解的物质保留了膜结合受体的许多特性。使用平衡透析测定法在4℃下测量[3H]甲硫氨酰-亮氨酰-苯丙氨酸与洋地黄皂苷提取物的结合。结合是可饱和的且具有高亲和力（Kd = 3.5 +/- 0.7 nM）。一系列合成肽作为[3H]甲硫氨酰-亮氨酰-苯丙氨酸与可溶性受体结合的抑制剂的效力顺序与对膜结合受体的抑制顺序相同。此外，与两种制剂的结合均依赖于巯基，对氯汞苯磺酸盐表现出平行抑制作用，随后用二硫苏糖醇孵育可部分逆转这种抑制作用。
