Biomaterial Database

Hemin regulation of hemoglobin binding by Porphyromonas gingivalis. 1998

J W Smalley, and A J Birss, and A S McKee, and P D Marsh

Unit of Oral Biology, Department of Clinical Dental Sciences, The University of Liverpool, Liverpool L69 3BX, UK.

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.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D010084	Oxidation-Reduction	A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).	Redox,Oxidation Reduction
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D002417	Cattle	Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.	Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D004305	Dose-Response Relationship, Drug	The relationship between the dose of an administered drug and the response of the organism to the drug.	Dose Response Relationship, Drug,Dose-Response Relationships, Drug,Drug Dose-Response Relationship,Drug Dose-Response Relationships,Relationship, Drug Dose-Response,Relationships, Drug Dose-Response
D006427	Hemin	Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.	Ferriprotoporphyrin,Hematin,Alkaline Hematin D-575,Chlorohemin,Ferrihaem,Ferriheme Chloride,Ferriprotoporphyrin IX,Ferriprotoporphyrin IX Chloride,Panhematin,Protohemin,Protohemin IX,Alkaline Hematin D 575,Chloride, Ferriheme,Chloride, Ferriprotoporphyrin IX,Hematin D-575, Alkaline
D006454	Hemoglobins	The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.	Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D016966	Porphyromonas gingivalis	A species of gram-negative, anaerobic, rod-shaped bacteria originally classified within the BACTEROIDES genus. This bacterium produces a cell-bound, oxygen-sensitive collagenase and is isolated from the human mouth.	Bacteroides gingivalis