Results 141 to 150 of about 6,249 (178)
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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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Hemopexin in newborn infants of diabetic mothers
Canadian Journal of Physiology and Pharmacology, 1968Serum proteins from cord blood of 27 infants of diabetic and 16 infants of normal women of comparable gestational age (38–39 weeks) were studied by immunoelectrophoresis. In accord with our previous finding of elevated serum glycoprotein levels in newborn infants of diabetic mothers, a well-defined precipitation arc in the beta-one globulin region ...
O V, Sirek, A, Sirek, A, Bucalossi
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Hemopexin is localized to human chromosome 11
Somatic Cell and Molecular Genetics, 1987Hemopexin, a plasma protein that migrates during electrophoresis with the beta-globulins, transports free heme to sites of its catabolism in the liver. A hemopexin cDNA clone has been utilized for mapping the hemopexin (HPX) gene to human chromosome 11 in the region pter----p11 by somatic cell hybrid analysis.
S L, Naylor +4 more
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Coordination of Nitric Oxide by Heme—Hemopexin
Journal of Protein Chemistry, 1998Hemopexin, which acts as an antioxidant by binding heme (Kd < 1 pM), is synthesized by hepatic parenchymal cells, by neurons of the central and peripheral nervous systems, and by human retinal ganglia. Two key regulatory molecules, nitric oxide (.NO) and carbon monoxide (CO), both bind to heme proteins and since ferroheme-hemopexin binds CO, the ...
N, Shipulina +3 more
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Hemopexin, the heme-binding serum β-glycoprotein
La Ricerca in Clinica e in Laboratorio, 1974Hemopexin, a heme-binding serum protein, was first described by Neale et al in 1958.1 The high carbohydrate content and immunoelectrophoretic identity of this macromolecule led to its designation by Schultze et al. 2 as β1B-glycoprotein. The name “hemopexin”, given by Grabar et al.,3 reflects the ability of the protein to bind heme† in an equimolar ...
Ursula Muller-Eberhard, Ham Heng Liem
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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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Elevations of Hemopexin Levels in Neuromuscular Disease
Archives of Neurology, 1978Hemopexin, a serum glycoprotein that binds free heme and transports it to hepatic parenchymal cells, has been measured by radial immunodiffusion. We have confirmed elevation of serum hemopexin concentration in Duchenne's muscular dystrophy patients and carries, and demonstrated elevations in dermatomyositis/polymyositis and myasthenia gravis, but not ...
B T, Adornato +2 more
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Hemopexin: The primary specific carrier of plasma heme*
Biochemistry and Molecular Biology Education, 2002AbstractHemopexin (HPX) is the primary specific carrier of plasma heme and participates in its clearance by transport to the liver. After delivering the heme intracellularly, HPX is released intact into the bloodstream. HPX is formed by two four‐bladed β‐propeller domains, resembling two thick disks that lock together at a 90° angle; the face of the N ...
M. Mattu +4 more
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Interaction of hemopexin with water-soluble porphyrins
Archives of Biochemistry and Biophysics, 1976Abstract Polyacrylamide-gel electrophoresis and filtration on Bio-Gel P-10 indicate that rabbit hemopexin binds deuteroporphyrin and 2,4-disulfonic acid deuteroporphyrin (dsDp) but not ethylenediamine-substituted protoporphyrin. Formation of the dsDp-hemopexin complex, produces a red shift in Soret maxima from 402 to 426 nm.
T P, Conway, U, Muller-Eberhard
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Heme Scavenging and the Other Facets of Hemopexin
Antioxidants & Redox Signaling, 2010Hemopexin is an acute-phase plasma glycoprotein, produced mainly by the liver and released into plasma, where it binds heme with high affinity. Other sites of hemopexin synthesis are the nervous system, skeletal muscle, retina, and kidney. The only known receptor for the heme-hemopexin complex is the scavenger receptor, LDL receptor-related protein ...
TOLOSANO, Emanuela +4 more
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