Results 131 to 140 of about 6,249 (178)
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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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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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In Vivo Fate of Hemopexin and Heme-Hemopexin Complexes in the Rat
Archives of Biochemistry and Biophysics, 1993The disposition in the rat of the plasma heme-binding protein hemopexin (Hx), as the native apoprotein and as its heme complex (HHx), has been studied using the residualizing protein label dilactitol-125I-tyramine (*I-DLT). The aim of this work was to identify the tissue sites of Hx uptake and catabolism, independent of heme binding, and to evaluate ...
Potter, David W. +7 more
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Revisiting the interaction of heme with hemopexin
Biological Chemistry, 2021Abstract In hemolytic disorders, erythrocyte lysis results in massive release of hemoglobin and, subsequently, toxic heme. Hemopexin is the major protective factor against heme toxicity in human blood and currently considered for therapeutic use. It has been widely accepted that hemopexin binds heme with extraordinarily high affinity of &
Milena Sophie Detzel +7 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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Nitrosylation of rabbit ferrous heme-hemopexin
JBIC Journal of Biological Inorganic Chemistry, 2004Hemopexin (HPX) serves as a trap for toxic plasma heme, ensuring its complete clearance by transportation to the liver. Moreover, HPX-heme has been postulated to play a key role in the homeostasis of nitric oxide (NO). Here, the thermodynamics for NO binding to rabbit ferrous HPX-heme as well as the EPR and optical absorption spectroscopic properties ...
Fasano M. +4 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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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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Immunological cross-reactions between heterologous hemopexins
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19781. The degree of immunological identity of the hemopexin of 64 mammals and non-mammals is determined by double diffusion in agar and two radioimmunoassays, employing antisera produced with the human or the rabbit protein. 2. Antigenic determinants are shared by the Eutherian mammals but not by the non-Eutherian mammals and lower animals. 3.
K H, Cox +4 more
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1980
There is a significant amount of methemoglobin circulating in human plasma at all times. In this compound, the iron in the iron-porphyrin complex is in the trivalent state and does not participate in oxygen exchange. The prosthetic group is called ferriprotoporphyrin IX. The free base is called hematin, and the chloride salt hemin (see Volume 2, p. 469)
Samuel Natelson, Ethan A. Natelson
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There is a significant amount of methemoglobin circulating in human plasma at all times. In this compound, the iron in the iron-porphyrin complex is in the trivalent state and does not participate in oxygen exchange. The prosthetic group is called ferriprotoporphyrin IX. The free base is called hematin, and the chloride salt hemin (see Volume 2, p. 469)
Samuel Natelson, Ethan A. Natelson
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