Hemoglobin binding activity and hemoglobin-binding protein of Prevotella nigrescens

European Journal of Medical Research

S Fujimura²  Y Shibata³  K Hirai²  O Ueda²  Y Kikuchi²  A Kiso¹  S Oishi¹  M Miyashita¹ 

[1] Department of Oral Health Promotion, Graduate School of Oral Medicine, Matsumoto Dental University, Shiojiri-Nagano, Japan;Department of Oral Microbiology, Matsumoto Dental University, Shiojiri-Nagano, Japan;Division of Oral Health Promotion, Institute for Oral Science, Matsumoto Dental University, Shiojiri-Nagano, Japan

关键词: anaerobe;    purification;    hemoglobin-binding protein;    hemoproteins;    hemoglobin;    Prevotella nigrescens;    periodontal pathogen;    iron acquisition;   

Others  :  834438
DOI  :  10.1186/2047-783X-15-7-314

 received in 2009-10-29, accepted in 2010-01-25,  发布年份 2010

【 摘 要 】

Prevotella nigrescens, lacking siderophores was found to bind to the hemoproteins. The binding was observed also in the envelope which was prepared by sonication of the cell. The binding occurred in the pH-dependent manner; the binding was observed below neutral pHs of the incubation mixtures but only slightly observed in the neutral and alkaline pHs. Furthermore, hemoglobin bound to the envelope was dissociated at high pHs buffers. Maximum amounts of hemoglobin bound to 1 mg envelope was 51.2 μg. Kd for the reaction at pH 5.0 was 2.1 × 10^-10M (210 pM). From the dot blot assay, hemoglobin could bind to a protein solubilized from the envelope by a detergent, referred to as hemoglobin-binding protein (HbBP), then it was purified by the sequential procedures of ion exchange chromatography, affinity chromatography and isoelectric focusing. Molecular weight and isoelectric point of the HbBP were 46 kDa and 6.1, respectively.

【 授权许可】

   
2010 I. Holzapfel Publishers

【 图 表 】

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