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Topic: Hemoglobin

Related Topics

Red blood cell

Hemocyanin

Hemoglobin F

Hemerythrin

Ferryl

Bohr effect

Methemoglobin

Oxyhemoglobin dissociation curve

Full blood count

Heme

Allosteric

Mean cell hemoglobin

Hematocrit

Iron deficiency anemia

Anaemia

	Hemoglobin - Wikipedia, the free encyclopedia
		Hemoglobin transports oxygen from the lungs to the rest of the body, such as to the muscles, where it releases the oxygen load.
		The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecule.
		This control of hemoglobin's affinity for oxygen by the binding and release of carbon dioxide and acid, is known as the Bohr effect.
	en.wikipedia.org /wiki/Hemoglobin (2297 words)

	Hemoglobin - MSN Encarta
		Hemoglobin controls the expansion and contraction of blood vessels, and thus blood pressure, by regulating the amount of nitric oxide to which the vessels are exposed.
		Hemoglobin is contained entirely in the red blood cells, amounting to perhaps 35 percent of their weight.
		After a life of perhaps 120 days, red blood cells are destroyed in the spleen, or in the course of circulation, their hemoglobin is broken into its constituents, including iron, which enters new blood cells formed in the bone marrow.
	encarta.msn.com /encyclopedia_761567357/Hemoglobin.html (402 words)

	Fetal hemoglobin - Wikipedia, the free encyclopedia
		Fetal hemoglobin (also hemoglobin F or HbF) is the main oxygen transport protein in the fetus during the last seven months of development in the womb.
		Functionally, fetal hemoglobin differs most from adult hemoglobin in that it is able to bind oxygen with greater affinity than the adult form, giving the developing fetus better access to oxygen from the mother's bloodstream.
		This variety of hemoglobin causes red blood cells to change their shape from round to sickle-shaped, which have a greater tendency to stack on top of one another and crowd blood vessels.
	en.wikipedia.org /wiki/Fetal_hemoglobin (733 words)

	Myoglobin and Hemoglobin
		Adult hemoglobin is a [a(2):b(2)] tetrameric hemeprotein found in erythrocytes where it is responsible for binding oxygen in the lung and transporting the bound oxygen throughout the body where it is used in aerobic metabolic pathways.
		The major hemoglobin at this stage of development is a tetramer composed of 2 zeta (z) chains encoded within the a cluster and 2 eta (e) chains from the b cluster.
		Hemoglobin Gun Hill is the result of a deletion of 15 nucleotides caused by unequal cross over between codons 91-94 of one b-globin gene and codons 96-98 of the other.
	web.indstate.edu /thcme/mwking/hemoglobin-myoglobin.html (4119 words)

	Structure/Function Relationships of Hemoglobin
		Hemoglobin’s primary function is to bind oxygen that diffuses into the bloodstream from the lungs and then transport it to outlying tissues where it is released primarily for aerobic respiration.
		Equally important, hemoglobin also manifests cooperativity in the reverse direction: When environmental oxygen levels are low, hemoglobin’s affinity for oxygen drops disproportionately as fewer and fewer oxygen molecules remain to bind to hemoglobin.
		Without hemoglobin’s specialized cooperative ligand binding behavior, nearly twice as much hemoglobin would be needed to transport the same amount of oxygen and this requirement would presumably require twice the blood volume to accommodate a doubling of the number of red blood cells for housing the additional hemoglobin.
	tutor.lscf.ucsb.edu /instdev/sears/biochemistry/tw-hbn/hba-overview.htm (700 words)

	hemoglobin (Site not responding. Last check: 2007-10-21)
		Hemoglobin is the oxygen-carrying molecule of the red blood cells, which are essentially just tiny circulating bags of hemoglobin.
		After the first few months of life hemoglobin F is almost totally replaced by the normal adult type hemoglobin A. Certain diseases are characterised by abnormal hemoglobin types, for example sickle cell disease.
		In this disease, an abnormal molecule known as hemoglobin S causes severe effects of capillary blood vessel blockage; another variant, hemoglobin C is common as well and causes similar disease as classic hemoglobin S sickling, but this condition is not as severe.
	www.drhull.com /EncyMaster/H/hemoglobin.html (163 words)

	Hemoglobin- Health Encyclopedia and Reference
		Hemoglobin is the iron-carrying protein found in red blood cells that binds to oxygen.
		Hemoglobin is a crystallizable, conjugated protein consisting of an iron-containing pigment (called heme or hematin) and a simple protein, globin.
		The principal function of hemoglobin is to combine and transport oxygen from the lungs following inhalation, and then deliver it to all body tissues, where it is required to provide energy for the chemical reactions of all living cells.
	drdean.healthcentral.com /encyclopedia/408/92/Hemoglobin.html (643 words)

	Hemoglobin and Cooperativity (Site not responding. Last check: 2007-10-21)
		Normal adult hemoglobin is composed of four subunits linked together, with each subunit containing a single heme -- the ring-like structure with a central iron atom that binds to an oxygen atom.
		In this ribbon model of hemoglobin, each of the four subunits is shown in a different color; the four heme groups are red.
		Hemoglobin structure is known for both its deoxygenated state, when it has no oxygen, and its oxygenated form -- carrying a full load of four oxygen atoms.
	www.psc.edu /science/Ho/Ho-hemoglobin.html (284 words)

	Hemoglobin Overview
		This brief overview of hemoglobin is not meant to be comprehensive.
		Hemoglobin is a protein that is carried by red cells.
		The hemoglobin inside the red cells of a person with type O blood and that inside the red cells of a person with type A blood are identical.
	sickle.bwh.harvard.edu /hemoglobin.html (778 words)

	hemoglobin articles on Encyclopedia.com (Site not responding. Last check: 2007-10-21)
		hemoglobin HEMOGLOBIN [hemoglobin], respiratory protein found in the red blood cells (erythrocytes) of all vertebrates and some invertebrates.
		A hemoglobin molecule is composed of a protein group, known as globin, and four heme groups, each associated with an iron atom.
		Such a condition is caused by a deficient number of erythrocytes (red blood cells), an abnormally low level of hemoglobin in the individual cells, or both these conditions simultaneously.
	www.encyclopedia.com /articlesnew/05803.html (475 words)

	Hemoglobin Synthesis
		With the exception of the first 10 to 12 weeks after conception, fetal hemoglobin is the primary hemoglobin in the developing fetus.
		Complex biophysical characteristics of the hemoglobin tetramer permit the exquisite control of oxygen uptake in the lungs and release in the tissues that is necessary to sustain life.
		The combination of two alpha genes and two beta genes comprises the normal adult hemoglobin, hemoglobin A. The delta gene, which is located between the gamma and beta genes on chromosome 11 produces a small amount of delta globin in children and adults.
	sickle.bwh.harvard.edu /hbsynthesis.html (1077 words)

	Hemoglobin Test \| AHealthyMe.com
		Hemoglobin is a protein inside red blood cells that carries oxygen throughout the body.
		Hemoglobin is made of heme, an iron compound, and globin, a protein.
		Hemoglobin is often ordered as part of a complete blood count (CBC), a test that includes other blood cell measurements.
	www.ahealthyme.com /topic/topic100586922 (655 words)

	Optical Absorption of Hemoglobin
		One equivalent of hemoglobin is assumed to be 64,500/4 or 16,125 gm.
		The red blood cells are primarily composed of hemoglobin (95% of the dry mass).
		When arterial blood is 90% saturated, some of the hemoglobin molecules have four oxygens bound, some have three, and a few have tow or one.
	omlc.ogi.edu /spectra/hemoglobin (404 words)

	Hemoglobin Home
		Hemoglobin is a tetramer composed of 4 globin molecules; 2 alpha globins and 2 beta globins.
		This regulation is known as cooperativity and is essential to the functioning of the hemoglobin because it allows the oxyhemoglobin to carry the maximum amount of oxygen to the tissues and then allows the deoxyhemoglobin to release the maximum amount of oxygen into the tissues (Sears, 1999).
		The hemoglobins of the bar-headed goose have been sequenced and compared to close relatives that do not live at high elevations and it was found that there were 4 main mutations between the hemoglobin molecules.
	www.bio.davidson.edu /Courses/Molbio/MolStudents/spring2005/Heiner/hemoglobin.html (1648 words)

	Hemoglobin
		The process whereby hemoglobin performs this essential physiological role is characterized by a cooperative interaction among its constituent subunits.
		Hemoglobin has thus assumed the role of a model system whose study acquires ramifications extending far beyond its own function as an oxygen transport system.
		The hemoglobin molecule is nearly spherical, with a diameter of 55 angstroms.
	biology.kenyon.edu /BMB/Chime/Lisa/FRAMES/hemetext.htm (965 words)

	Hemoglobin - Health and Medical Information produced by doctors - MedicineNet.com
		Hemoglobin is the protein molecule in red blood cells that carries oxygen from the lungs to the body's tissues and returns carbon dioxide from the tissues to the lungs.
		The free hemoglobin is exposed to a chemical containing cyanide which binds tightly with the hemoglobin molecule to form cyanmethemoglobin.
		The hemoglobin level is expressed as the amount of hemoglobin in grams (gm) per deciliter (dl) of whole blood, a deciliter being 100 milliliters.
	www.medicinenet.com /hemoglobin/article.htm (476 words)

	Hemoglobin Info - Encyclopedia WikiWhat.com (Site not responding. Last check: 2007-10-21)
		The molecule is mostly protein: mutations in the gene for the haemoglobin protein result in the hereditary diseases sickle cell anaemia and thalassaemia, as well as a group of diverse but rare diseases called hemoglobinopathies.
		A structure of deoxy human hemoglobin is given by PDB 1A3N.
		In the tetrameric form of normal adult hemoglobin, the binding of oxygen is a cooperative process, with the binding affinity of hemoglobin for oxygen affected by the oxygen saturation of the molecule.
	wikiwhat.com /encyclopedia/h/he/hemoglobin.html (725 words)

	Hemoglobin Electrophoresis
		A hemoglobin electrophoresis test is a blood test done to evaluate the different types of hemoglobin in the bloodstream.
		Hemoglobin F is replaced by hemoglobin A (adult hemoglobin) shortly after birth; only very small amounts of hemoglobin F are produced after birth.
		Hemoglobin S and hemoglobin C are the most common types of abnormal hemoglobins that may be identified by an electrophoresis test.
	www.webmd.com /hw/health_guide_atoz/hw39098.asp (1064 words)

	hemoglobin
		Hemoglobin is found in erythrocytes where it is responsible for binding oxygen in the lung and transporting the bound oxygen throughout the body where it is used in aerobic metabolic pathways.
		In addition, the quaternary structure of hemoglobin leads to physiologically important allosteric interactions between the subunits, a property lacking in monomeric myoglobin which is otherwise very similar to the b-subunit of hemoglobin.
		illustrate the allosteric properties of hemoglobin that results from its quaternary structure and differentiate hemoglobin's oxygen binding properties from that of myoglobin.
	www.med.unibs.it /~marchesi/hemoglob.html (1449 words)

	Fetal Hemoglobin (Hemoglobin F) Fact Sheet (Site not responding. Last check: 2007-10-21)
		Fetal hemoglobin (hemoglobin F) is the main hemoglobin that transports oxygen around the body of the developing baby during the last 7 months of pregnancy.
		Fetal hemoglobin is best suited to the conditions in the womb and the oxygen transport needs of babies still in their mothers' wombs.
		Hemoglobin A is better suited to the oxygen transport needs after birth and throughout adult life.
	www.fha.state.md.us /genetics/html/hemo_f.html (273 words)

	Glycosylated hemoglobin (Site not responding. Last check: 2007-10-21)
		When measured with chromatography, glycosylated hemoglobin in whole blood is stable for 7 days at 4 C and for 3 days at 25 C. When measured by thiobarbituric acid colorimetry, glycosylated hemoglobin is stable in whole blood for 21 days at 4 C and room temperature.
		Therefore, glycosylated hemoglobin is an indicator of the blood glucose concentration over a longer period of time than either a single blood glucose measurement (which reflects the glucose concentration at the time of blood collection) or fructosamine concentrations.
		Assay method: Cats have variable amounts of hemoglobin B as well as hemoglobin A. Ion-exchange chromatography methods are specific for hemoglobin A and may, therefore, underestimate glycosylated hemoglobin concentrations in cats.
	www.diaglab.vet.cornell.edu /clinpath/modules/chem/glycos.htm (400 words)

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