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Growth inhibition of Bacteroides fragilis by hemopexin: proteolytic degradation of hemopexin to overcome heme limitation [PDF]
FEMS Microbiology Letters, 2001 The stimulatory effect of heme on growth of Bacteroides fragilis, an anaerobic human pathogen, was strongly inhibited by hemopexin, an avid ...
Ann Smith, Edson R Rocha, Smith Ann
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Vox Sanguinis, 1968
Summary. It has been shown that a genetically controlled polymorphic protein of rabbit serum is soluble in 0.6N HClO4 and complexes with heme and not hemoglobin. It is proposed that the name of this protein be changed from heme‐binding protein to hemopexin in order to identify it with serum proteins of other species which exhibit similar properties ...
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Summary. It has been shown that a genetically controlled polymorphic protein of rabbit serum is soluble in 0.6N HClO4 and complexes with heme and not hemoglobin. It is proposed that the name of this protein be changed from heme‐binding protein to hemopexin in order to identify it with serum proteins of other species which exhibit similar properties ...
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On the heme-binding capacity of hemopexin
Clinica Chimica Acta, 1964Abstract Hemopexin, a β 1 -globulin from human serum, forms with hemin a red-coloured complex which consists of one mole of hemopexin and one mole of hemin. This complex is stable in the presence of albumin. The composition of the hemopexinhemin complex has been investigated with the aid of spectrophotometric, starch gel and iron analysis. This study
K, HEIDE +3 more
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Interaction of rabbit hemopexin with bilirubin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978The interaction of hemopexin with bilirubin was characterized by spectrophotometric, fluorimetric and circular dichroic techniques. Hemopexin rapidly forms an equimolar complex with libirubin that has an apparent dissociation constant Kd, of 7.5.10(-7) M.
W T, Morgan +2 more
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Identification of hemopexin in tear film
Analytical Biochemistry, 2010Human tear fluid is a complex mixture of aqueous lipids, proteins, enzymes, and other biochemical and cellular elements. By conventional comparative proteomic approaches, we investigated the proteome in human tear fluid and compared the tear protein profile of normal control subjects with that of patients suffering from the ocular inflammatory disease ...
Jeffrey C F, Pong +6 more
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Characterization of sheep hemopexin glycovariants
Glycoconjugate Journal, 1995The hemopexin phenotype HpxB1 isolated from sheep serum, yields three major bands when subjected to starch gel and/or polyacrylamide gel electrophoresis which are here designated as subcomponents HpxB1-I, HpxB1-II and HpxB1-III. Electrospray mass spectrometric analysis of samples of the isolated subcomponents prepared by ion exchange chromatography ...
B, Coddeville +5 more
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Hemopexin: Structure, Function, and Regulation
DNA and Cell Biology, 2002Hemopexin (HPX) is the plasma protein with the highest binding affinity to heme among known proteins. It is mainly expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially highly toxic because of its ability to intercalate into lipid membrane and to produce hydroxyl radicals ...
Emanuela, Tolosano, Fiorella, Altruda
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Structural studies on porcine hemopexin
International Journal of Biochemistry, 19901. Porcine hemopexin was isolated from the serum of a single animal and purified to homogeneity. 2. Porcine hemopexin has an apparent Mw of 67,000, binds heme in a 1:1 molar ratio and consists of 24% N-linked oligosaccharides. The amino acid composition of porcine hemopexin compares well with the amino acid composition of human and rabbit hemopexins. 3.
H T, Spencer, M J, Pete, D R, Babin
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Depletion of Serum Hemopexin in Fulminant Rhabdomyolysis
Archives of Neurology, 1978Hemopexin is a normal serum glycoprotein that functions as a carrier for intravascularly liberated free heme. Although its role is well established in the reutilization of hemoglobin-derived heme, there have been no previous clinical data to support its suspected interaction with heme released in the degradation of myoglobin.
B T, Adornato +3 more
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Metal Ion Binding to Human Hemopexin
Biochemistry, 2005Binding of divalent metal ions to human hemopexin (Hx) purified by a new protocol has been characterized by metal ion affinity chromatography and potentiometric titration in the presence and absence of bound protoheme IX. ApoHx was retained by variously charged metal affinity chelate resins in the following order: Ni(2+) > Cu(2+) > Co(2+) > Zn(2+) > Mn(
Marcia R, Mauk +4 more
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