エリスロクルオリン
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/11/24 00:33:42」(JST)
[Wiki en表示]
Erythrocruorin is a large oxygen-carrying protein, whose molecular mass is greater than 3.5 million Daltons[1]. It is related to the similar chlorocruorin. It is found in many annelids.
References[edit]
- "Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids", PNAS June 20, 2000. Accessed July 17, 2007.
External links[edit]
- Erythrocruorins at the US National Library of Medicine Medical Subject Headings (MeSH)
Proteins: hemeproteins
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Globins |
Hemoglobin
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Subunits
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Alpha locus on 16: α (HBA1, HBA2) · ζ (HBZ) · θ (HBQ1) · μ (HBM)
Beta locus on 11: β (HBB) · δ (HBD) · γ (HBG1, HBG2) · ε (HBE1)
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Tetramers
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stages of development: HbA (α2β2) · HbA2 (α2δ2) · HbF/Fetal (α2γ2) · HbE Gower 2 (α2ε2) · HbE Gower 1 (ζ2ε2)
pathology: HbH (β 4) · Barts (γ 4) · HbS (α 2β S2) · HbC (α 2β C2) · HbE (α 2β E2)
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Compounds
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Carboxyhemoglobin · Carbaminohemoglobin · Oxyhemoglobin/Deoxyhemoglobin · Sulfhemoglobin
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Other human
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Glycated hemoglobin · Methemoglobin
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Nonhuman
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Chlorocruorin · Erythrocruorin
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Other
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human: Myoglobin (Metmyoglobin) · Neuroglobin · Cytoglobin
plant: Leghemoglobin
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Other |
Cytochrome (Cytochrome b, Cytochrome P450) · Hemocyanin · Methemalbumin
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see also disorders of globin and globulin proteins
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cell/phys (coag, heme, immu, gran), csfs
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rbmg/mogr/tumr/hist, sysi/epon, btst
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drug (B1/2/3+5+6), btst, trns
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UpToDate Contents
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English Journal
- Evaluating the capacity to generate and preserve nitric oxide bioactivity in highly purified earthworm erythrocruorin: a giant polymeric hemoglobin with potential blood substitute properties.
- Roche CJ1, Talwar A2, Palmer AF3, Cabrales P4, Gerfen G1, Friedman JM5.
- The Journal of biological chemistry.J Biol Chem.2015 Jan 2;290(1):99-117. doi: 10.1074/jbc.M114.583260. Epub 2014 Nov 4.
- The giant extracellular hemoglobin (erythrocruorin) from the earth worm (Lumbricus terrestris) has shown promise as a potential hemoglobin-based oxygen carrier (HBOC) in in vivo animal studies. An important beneficial characteristic of this hemoglobin (LtHb) is the large number of heme-based oxygen
- PMID 25371199
- The self-association of the giant hemoglobin from the earthworm, Lumbricus terrestris.
- Riggs AF1, Riggs CK2.
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Jun;1844(6):1071-5. doi: 10.1016/j.bbapap.2014.03.004. Epub 2014 Mar 12.
- BACKGROUND: The crystallographic structure of the gigantic hemoglobin (erythrocruorin) of the annelid worm, Lumbricus terrestris, provides a molar mass of 3.6MDa for the hexagonal bilayer structure. Prior to this determination, some light-scattering and ultracentrifugal measurements indicated higher
- PMID 24631544
- Oxygen delivery during extreme anemia with ultra-pure earthworm hemoglobin.
- Elmer J1, Palmer AF, Cabrales P.
- Life sciences.Life Sci.2012 Oct 29;91(17-18):852-9. doi: 10.1016/j.lfs.2012.08.036. Epub 2012 Sep 13.
- AIM: Lumbricus terrestris (earthworm) erythrocruorin (LtEc) is a naturally occurring extracellular hemoglobin (Hb) with high molecular weight (3.6MDa), low autoxidation rate, and limited nitric oxide (NO) dioxygenation activity. These properties make LtEc a potential candidate for use as red blood c
- PMID 22982347
Japanese Journal
- Crystal structure of hemoglobin dodecamer from Lumbricus erythrocruorin : Allosteric core of giant Annelid respiratory complexes
- Effects of Magnesium and Calcium on the Oxygenation Reaction of Erythrocruorin from the Marine Polychaete Arenicola marina and the Terrestrial Oligochaete Lumbricus terrestris(Physiology)
- Ochiai Takehiko,Weber Roy E.
- Zoological science 19(9), 995-1000, 2002-09-25
- … Oxygenation function of annelid erythrocruorin (Er) is affected by Mg and Ca concentration in the blood. …
- NAID 110003372803
Related Links
- Forms and Functions The huge earthworm erythrocruorin, and the smaller human hemoglobin shown here at the bottom right (PDB entry 2hhb), are used primarily to transport oxygen. The large hemoglobin made by tubeworms ...
- erythrocruorin [ə‚rith·rə′kru ·ə·rən] (biochemistry) Any of the iron-porphyrin protein respiratory pigments found in the blood and tissue fluids of certain invertebrates; corresponds to hemoglobin in vertebrates. Erythrocruorin a hemoglobin ...
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