De Nardin E, Radel S J, Genco R J
Department of Oral Biology, State University of New York, Buffalo.
Biochem Biophys Res Commun. 1991 Jan 15;174(1):84-9. doi: 10.1016/0006-291x(91)90488-s.
The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and approximately 40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa greater than approximately 40 kDa greater than 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP.
据报道，诸如FMLP等甲酰化肽的受体由分子量在24至95 kDa之间的糖蛋白成分组成，并且对配体表现出高亲和力和低亲和力。关于这些成分的分子大小、数量以及不同亲和力是否代表不同的配体结合位点，存在争议。在本研究中，发现该受体由分子量分别为94 kDa、68 kDa和约40 kDa的成分组成。竞争性结合抑制实验表明，FMLP与这些成分的结合亲和力从高到低依次为：68 kDa大于约40 kDa大于94 kDa。我们的研究结果表明，人中性粒细胞的FMLP受体至少包含三种成分，并且每种成分对FMLP具有不同的亲和力。
