Osland A, Endresen C
Department of Microbiology and Immunology, Gade Institute, University of Bergen, Norway.
Zentralbl Bakteriol Mikrobiol Hyg A. 1988 Jun;268(4):435-47. doi: 10.1016/s0176-6724(88)80121-4.
A high density lipoprotein (HDL) binding component from the cell wall of Staphylococcus capitis, possessing both HDL binding and HDL precipitating activity, has been partially characterised. Growth of the bacteria on medium containing cysteine or in presence of CO2, was found to induce the synthesis of this factor. Analysis show an incorporation of radioactive amino acids into the factor, and also its sensitivity to trypsin, indicating strongly that the HDL binding factor is of protein nature. Gel-filtration experiments showed that the HDL binding protein had an elution volume corresponding to a molecular weight of about 150K. However, SDS-PAGE analysis of HDL binding protein, purified by affinity chromatography, showed that the 150K component was composed of subunits of a low molecular weight protein (7K). As judged by the incorporation of radiolabelled amino acids, the HDL binding protein may, under certain growth conditions, constitute as much as 15% of the total protein in the autolytic extract from the bacteria.
来自头状葡萄球菌细胞壁的一种高密度脂蛋白（HDL）结合成分已得到部分特性鉴定，该成分兼具HDL结合和HDL沉淀活性。研究发现，细菌在含有半胱氨酸的培养基上生长或在二氧化碳存在的条件下生长时，会诱导这种因子的合成。分析表明，放射性氨基酸掺入了该因子，并且它对胰蛋白酶敏感，这有力地表明HDL结合因子具有蛋白质性质。凝胶过滤实验表明，HDL结合蛋白的洗脱体积对应于约150K的分子量。然而，对通过亲和色谱纯化的HDL结合蛋白进行的SDS-PAGE分析表明，150K的成分由低分子量蛋白（7K）的亚基组成。根据放射性标记氨基酸的掺入情况判断，在某些生长条件下，HDL结合蛋白可能占细菌自溶提取物中总蛋白的15%之多。
