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Nitrosylation of rabbit ferrous heme-hemopexin

JBIC Journal of Biological Inorganic Chemistry, 2004
Hemopexin (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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Hemopexin in newborn infants of diabetic mothers

Canadian Journal of Physiology and Pharmacology, 1968
Serum 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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Interaction of hemopexin with water-soluble porphyrins

Archives of Biochemistry and Biophysics, 1976
Abstract 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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Hemopexin is localized to human chromosome 11

Somatic Cell and Molecular Genetics, 1987
Hemopexin, 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, 1998
Hemopexin, 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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Heme Scavenging and the Other Facets of Hemopexin

Antioxidants & Redox Signaling, 2010
Hemopexin 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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Hemopexin: Iron Recycling

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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Elevations of Hemopexin Levels in Neuromuscular Disease

Archives of Neurology, 1978
Hemopexin, 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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Identification of hemopexin as a GH-regulated gene

Molecular and Cellular Endocrinology, 2003
A cDNA library from the liver of a growth hormone (GH)-treated hypophysectomized rat was constructed and screened for GH-inducible genes (GIGs). Three cDNAs specific for putative GIG mRNAs (GIG-3, -7 and -12) were isolated and, when sequenced, were found to be homologous to portions of rat hemopexin, a Class 2 acute-phase gene.
Susan E, Stred, Joseph L, Messina
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Hepatic uptake of heme and hemopexin but not albumin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1974
Abstract [ 3 H] Heme and 125 I-labeled hemopexin are taken up by the rabbit liver maximally 1 h after injection; 131 I-labeled albumin however is not taken up, even when heme circulates in excess of the heme-binding capacity of hemopexin. Thus, hepatic engulfment of heme in vivo appears to be facilitated by hemopexin but not by albumin.
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