heme


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Related to heme: heme protein, Heme iron, Heme oxygenase

heme

 [hēm]
the nonprotein, insoluble, iron protoporphyrin constituent of hemoglobin, of various other respiratory pigments, and of many cells, both animal and vegetable. It is an iron compound and constitutes the pigment portion or protein-free part of the hemoglobin molecule, and is responsible for its oxygen-carrying properties.

heme

(hēm),
1. The porphyrin chelate of iron in which the iron is Fe(II) (or Fe2+); the oxygen-carrying, color-furnishing, prosthetic group of hemoglobin.
2. Iron complexed with nonporphyrins but related tetrapyrrole structures (for example, biliverdin heme).
3. Iron chelated with any porphyrin, irrespective of the valence state of the iron atom.
[G. haima, blood]

heme

(hēm) an iron compound of protoporphyrin which constitutes the pigment portion or protein-free part of the hemoglobin molecule and is responsible for its oxygen-carrying properties.

heme

(hēm)
n.
A deep red, iron-containing compound, C34H32FeN4O4, that constitutes the nonprotein component of hemoglobin and certain other proteins.

heme

[hēm]
Etymology: Gk, haima, blood
the pigmented iron-containing nonprotein part of the hemoglobin molecule. There are four heme groups in a hemoglobin molecule, each consisting of a cyclic structure of four pyrrole residues, called protoporphyrin, and an iron ion in the center. Heme binds and carries oxygen in the red blood cells, releasing it to tissues. Also spelled haeme. See also hemoglobin, porphobilinogen, protoporphyrin.

heme

 An iron-containing red pigment which, with a protein, globin, forms hemoglobin

heme

(hēm)
1. The porphyrin chelate of iron in which the iron is Fe(II) (Fe2+); the oxygen-carrying, color-furnishing, prosthetic group of hemoglobin.
2. Iron complexed with nonporphyrins but related tetrapyrrole structures (e.g., biliverdin heme).
Synonym(s): reduced hematin, haem.
[G. haima, blood]

heme

see HAEM.

Heme

The iron-containing molecule in hemoglobin that serves as the site for oxygen binding.

heme

(hēm)
1. The oxygen-carrying, color-furnishing, prosthetic group of hemoglobin.
2. Iron complexed with nonporphyrins but related tetrapyrrole structures.
Synonym(s): reduced hematin, haem.
[G. haima, blood]

heme,

n the pigmented, iron-contain-ing, nonprotein portion of the hemoglobin molecule.

heme

the nonprotein, insoluble, iron protoporphyrin constituent of hemoglobin, of various other respiratory pigments, and of many cells, both animal and vegetable. It is an iron compound of protoporphyrin and so constitutes the pigment portion or protein-free part of the hemoglobin molecule, and is responsible for its oxygen-carrying properties.

heme pigment nephropathy
see hemoglobinuric nephrosis.
heme synthetase
the rate-controlling enzyme for the synthesis of heme.
References in periodicals archive ?
Cytoprotection behind heme oxygenase-1 in renal diseases.
Both haptoglobin and hemopexin ultimately deliver heme to the cells of the reticuloendothelial system, activating another protective process.
Although the study carefully teases apart the mechanism, researchers don't know how well heme oxygenase-1 works against malaria in people.
Este algoritmo leva em consideracao o teor de ferro heme e nao-heme e os fatores potencializadores de sua absorcao, especificamente as carnes ingeridas (tecido animal), gordura e vitamina C presentes na composicao de cada refeicao.
So it appears that overall beef color is mainly determined by the status of heme pigments, which is determined by the reducing potential of red meats.
IRON SOURCES Food Milligrams per serving HEME IRON Clams (7) 23.
Heme iron, derived from animal blood and muscle, is absorbed more readily than the nonheme iron found in plants and iron salts.
Heme iron, the type found in animal products, is absorbed much better by the body.
Whereas vegetables and grains provide good sources of non-heme iron, only 2-5% of non-heme i ron is absorbed, compared to 10-35% of heme iron derived from meats.
THE FERRIS Wheel at a War-rington t heme park is still closed to the public more than two monthsafter the death of a 15-year-old disabled girl.
The introduction of threonine into the distal heme pocket, despite having only small perturbations in the local structure, had a marked affect on the interaction with ligands.
And this diet contained none of the heme iron supplied by the typical U.