Myhre E B, Kronvall G
Infect Immun. 1980 Jan;27(1):6-14. doi: 10.1128/iai.27.1.6-14.1980.
A total of 297 bacterial strains belonging to 27 species was tested for quantitative uptake of radiolabeled human serum albumin. Specific binding sites with high affinity for human serum albumin were found exclusively in group C and G streptococci. The albumin binding was found to be a time-dependent, saturable, and displaceable process which obeyed simple kinetic equations. Scatchard analysis revealed that human serum albumin bound to a homogeneous population of receptors with an affinity in the order ot 10(7) liters/mol and that the average bacterial cell carried more than 80,000 binding sites. The albumin receptor is a heat-stable component susceptible to proteolytic digestion. It has a surface localization separate from the receptors for immunolgobulin G, fibrinogen, aggregated beta 2-microglobulin, and haptoglobin. In individual strains, albumin reactivity was also detected independently of these other types of interactions with human proteins.
对属于27个物种的总共297株细菌菌株进行了放射性标记人血清白蛋白的定量摄取测试。仅在C组和G组链球菌中发现了对人血清白蛋白具有高亲和力的特异性结合位点。发现白蛋白结合是一个时间依赖性、可饱和且可置换的过程，遵循简单的动力学方程。Scatchard分析表明，人血清白蛋白与亲和力约为10(7)升/摩尔的同质受体群体结合，并且平均细菌细胞携带超过80,000个结合位点。白蛋白受体是一种对蛋白水解消化敏感的热稳定成分。它具有与免疫球蛋白G、纤维蛋白原、聚集的β2-微球蛋白和触珠蛋白的受体分开的表面定位。在个别菌株中，也独立于与人类蛋白质的这些其他类型相互作用检测到白蛋白反应性。
