Results 171 to 180 of about 7,813 (203)
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Depletion of Serum Hemopexin in Fulminant Rhabdomyolysis

Archives of Neurology, 1978
Hemopexin 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
openaire   +2 more sources

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
openaire   +4 more sources

Metal Ion Binding to Human Hemopexin

Biochemistry, 2005
Binding 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
openaire   +2 more sources

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
openaire   +3 more sources

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
openaire   +2 more sources

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
openaire   +1 more source

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
openaire   +2 more sources

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
openaire   +2 more sources

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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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.
openaire   +2 more sources

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