Hemin regulation of hemoglobin binding by Porphyromonas gingivalis
Hemoglobin binding to chemostat-grown hemin-excess and hemin-limited cells of Porphyromonas gingivalis W50, and to cells of the avirulent, beige-pigmenting variant W50/BE1, was quantified. Hemin-excess W50 bound more hemoglobin than hemin-limited W50, mirroring the hemin-binding ability of these cel...
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| Veröffentlicht in: | Current microbiology 1998-02, Vol.36 (2), p.102-106 |
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| creator | SMALLEY, J. W BIRSS, A. J MCKEE, A. S MARSH, P. D |
| description | Hemoglobin binding to chemostat-grown hemin-excess and hemin-limited cells of Porphyromonas gingivalis W50, and to cells of the avirulent, beige-pigmenting variant W50/BE1, was quantified. Hemin-excess W50 bound more hemoglobin than hemin-limited W50, mirroring the hemin-binding ability of these cells [Microb Ecol Health Dis 7:9-15, 1994]. In contrast to hemin, hemoglobin binding was not enhanced by sodium dithionite. The hemoglobin-binding capacity of hemin-excess W50/BE1 was below that of hemin-limited W50 and only observed under oxidizing conditions. Scatchard analysis revealed similar affinity constants for hemin-excess and hemin-limited W50, and confirmed a lower binding maximum for the latter. Hemin-excess W50/BE1 displayed cooperative binding of hemoglobin. These differences in binding were reflected in the binding of a horse radish peroxidase-conjugated hemoglobin (HHRPO) in a dot-blot assay. However, neither the 32-kDa hemin-binding protein, nor its 19-kDa heat-modified form, from either hemin-limited W50 or hemin-excess W50/BE1, bound this conjugate. These data indicate that hemoglobin binding by P. gingivalis is hemin-regulated and occurs via a mechanism different from hemin binding. |
| doi_str_mv | 10.1007/s002849900287 |
| format | Article |
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W ; BIRSS, A. J ; MCKEE, A. S ; MARSH, P. D</creator><creatorcontrib>SMALLEY, J. W ; BIRSS, A. J ; MCKEE, A. S ; MARSH, P. D</creatorcontrib><description>Hemoglobin binding to chemostat-grown hemin-excess and hemin-limited cells of Porphyromonas gingivalis W50, and to cells of the avirulent, beige-pigmenting variant W50/BE1, was quantified. Hemin-excess W50 bound more hemoglobin than hemin-limited W50, mirroring the hemin-binding ability of these cells [Microb Ecol Health Dis 7:9-15, 1994]. In contrast to hemin, hemoglobin binding was not enhanced by sodium dithionite. The hemoglobin-binding capacity of hemin-excess W50/BE1 was below that of hemin-limited W50 and only observed under oxidizing conditions. Scatchard analysis revealed similar affinity constants for hemin-excess and hemin-limited W50, and confirmed a lower binding maximum for the latter. Hemin-excess W50/BE1 displayed cooperative binding of hemoglobin. These differences in binding were reflected in the binding of a horse radish peroxidase-conjugated hemoglobin (HHRPO) in a dot-blot assay. However, neither the 32-kDa hemin-binding protein, nor its 19-kDa heat-modified form, from either hemin-limited W50 or hemin-excess W50/BE1, bound this conjugate. These data indicate that hemoglobin binding by P. gingivalis is hemin-regulated and occurs via a mechanism different from hemin binding.</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/s002849900287</identifier><identifier>PMID: 9425248</identifier><identifier>CODEN: CUMIDD</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Animals ; Bacteriology ; Biological and medical sciences ; Biotechnology ; Cattle ; Dose-Response Relationship, Drug ; Fundamental and applied biological sciences. 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Scatchard analysis revealed similar affinity constants for hemin-excess and hemin-limited W50, and confirmed a lower binding maximum for the latter. Hemin-excess W50/BE1 displayed cooperative binding of hemoglobin. These differences in binding were reflected in the binding of a horse radish peroxidase-conjugated hemoglobin (HHRPO) in a dot-blot assay. However, neither the 32-kDa hemin-binding protein, nor its 19-kDa heat-modified form, from either hemin-limited W50 or hemin-excess W50/BE1, bound this conjugate. These data indicate that hemoglobin binding by P. gingivalis is hemin-regulated and occurs via a mechanism different from hemin binding.</description><subject>Animals</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cattle</subject><subject>Dose-Response Relationship, Drug</subject><subject>Fundamental and applied biological sciences. 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W</au><au>BIRSS, A. J</au><au>MCKEE, A. S</au><au>MARSH, P. D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hemin regulation of hemoglobin binding by Porphyromonas gingivalis</atitle><jtitle>Current microbiology</jtitle><addtitle>Curr Microbiol</addtitle><date>1998-02-01</date><risdate>1998</risdate><volume>36</volume><issue>2</issue><spage>102</spage><epage>106</epage><pages>102-106</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><coden>CUMIDD</coden><abstract>Hemoglobin binding to chemostat-grown hemin-excess and hemin-limited cells of Porphyromonas gingivalis W50, and to cells of the avirulent, beige-pigmenting variant W50/BE1, was quantified. Hemin-excess W50 bound more hemoglobin than hemin-limited W50, mirroring the hemin-binding ability of these cells [Microb Ecol Health Dis 7:9-15, 1994]. In contrast to hemin, hemoglobin binding was not enhanced by sodium dithionite. The hemoglobin-binding capacity of hemin-excess W50/BE1 was below that of hemin-limited W50 and only observed under oxidizing conditions. Scatchard analysis revealed similar affinity constants for hemin-excess and hemin-limited W50, and confirmed a lower binding maximum for the latter. Hemin-excess W50/BE1 displayed cooperative binding of hemoglobin. These differences in binding were reflected in the binding of a horse radish peroxidase-conjugated hemoglobin (HHRPO) in a dot-blot assay. However, neither the 32-kDa hemin-binding protein, nor its 19-kDa heat-modified form, from either hemin-limited W50 or hemin-excess W50/BE1, bound this conjugate. These data indicate that hemoglobin binding by P. gingivalis is hemin-regulated and occurs via a mechanism different from hemin binding.</abstract><cop>New York, NY</cop><pub>Springer</pub><pmid>9425248</pmid><doi>10.1007/s002849900287</doi><tpages>5</tpages></addata></record> |
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| ispartof | Current microbiology, 1998-02, Vol.36 (2), p.102-106 |
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| subjects | Animals Bacteriology Biological and medical sciences Biotechnology Cattle Dose-Response Relationship, Drug Fundamental and applied biological sciences. Psychology Hemin - administration & dosage Hemin - pharmacology Hemoglobin Hemoglobins - chemistry Hemoglobins - metabolism Kinetics Membrane Proteins - chemistry Membrane Proteins - metabolism Microbiology Oxidation-Reduction Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Porphyromonas gingivalis - drug effects Porphyromonas gingivalis - metabolism Protein Binding - drug effects |
| title | Hemin regulation of hemoglobin binding by Porphyromonas gingivalis |
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