血红蛋白与牙龈卟啉单胞菌包膜的结合及血红蛋白结合蛋白的分离
Binding of hemoglobin to the envelope of Porphyromonas gingivalis and isolation of the hemoglobin-binding protein.
作者信息
Fujimura S, Shibata Y, Hirai K, Nakamura T
机构信息
Department of Oral Microbiology, Matsumoto Dental College, Shiojiri-Shi, Nagano-Ken, Japan.
出版信息
Infect Immun. 1996 Jun;64(6):2339-42. doi: 10.1128/iai.64.6.2339-2342.1996.
Abstract
The binding activity of the Porphyromonas gingivalis envelope and hemoglobin was examined over a wide range of pH values from 4.5 to 9.0. The binding activity in low-pH buffers was much higher than that at high pH; the optimum pHs for the binding were found to be 4.5 and 5.0. Since the hemoglobin bound to the envelope was found to dissociate in the pH 8.5 and 9.0 buffers, the binding is reversible. We hypothesized that hemoglobin-binding protein (HbBP), responsible for the binding to hemoglobin, exists in the envelope and confirmed its presence by dot blot determination with peroxidase-conjugated hemoglobin. Then we attempted to isolate HbBP from the solubilized (by a detergent) materials of the envelope by affinity chromatography. The molecular mass of HbBP was 19 kDa, and the isoelectric point was 4.3.
摘要
在4.5至9.0的广泛pH值范围内检测了牙龈卟啉单胞菌包膜与血红蛋白的结合活性。低pH缓冲液中的结合活性远高于高pH时的结合活性；发现结合的最佳pH值为4.5和5.0。由于发现与包膜结合的血红蛋白在pH 8.5和9.0缓冲液中会解离，因此这种结合是可逆的。我们推测负责与血红蛋白结合的血红蛋白结合蛋白（HbBP）存在于包膜中，并通过过氧化物酶偶联血红蛋白的斑点印迹测定法证实了其存在。然后我们尝试通过亲和色谱从包膜的可溶解（用去污剂）材料中分离HbBP。HbBP的分子量为19 kDa，等电点为4.3。
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