Hemoglobin in the context of Gill


Hemoglobin in the context of Gill

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⭐ Core Definition: Hemoglobin

Hemoglobin (haemoglobin, Hb or Hgb) is a protein containing iron that facilitates the transportation of oxygen in red blood cells. Almost all vertebrates contain hemoglobin, with the sole exception of the fish family Channichthyidae. Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and a globulin.

In mammals, hemoglobin makes up about 96% of a red blood cell's dry weight (excluding water), and around 35% of the total weight (including water). Hemoglobin has an oxygen-binding capacity of 1.34 mL of O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. The mammalian hemoglobin molecule can bind and transport up to four oxygen molecules.

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Hemoglobin in the context of Potassium nitrate

Potassium nitrate is a chemical compound with a sharp, salty, bitter taste and the chemical formula KNO3. It is a potassium salt of nitric acid. This salt consists of potassium cations K and nitrate anions NO3, and is therefore an alkali metal nitrate. It occurs in nature as a mineral, niter (or nitre outside the United States). It is a source of nitrogen, and nitrogen was named after niter. Potassium nitrate is one of several nitrogen-containing compounds collectively referred to as saltpetre (or saltpeter in the United States).

Major uses of potassium nitrate are in fertilizers, tree stump removal, rocket propellants and fireworks. It is one of the major constituents of traditional gunpowder (black powder). In processed meats, potassium nitrate reacts with hemoglobin and myoglobin generating a red color.

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Hemoglobin in the context of Blood

Blood is a body fluid in the circulatory system of humans and other vertebrates that delivers necessary substances such as nutrients and oxygen to the cells, and transports metabolic waste products away from those same cells.

Blood is composed of blood cells suspended in plasma. Plasma, which constitutes 55% of blood fluid, is mostly water (92% by volume), and contains proteins, glucose, mineral ions, and hormones. The blood cells are mainly red blood cells (erythrocytes), white blood cells (leukocytes), and (in mammals) platelets (thrombocytes). The most abundant cells are red blood cells. These contain hemoglobin, which facilitates oxygen transport by reversibly binding to it, increasing its solubility. Jawed vertebrates have an adaptive immune system, based largely on white blood cells. White blood cells help to resist infections and parasites. Platelets are important in the clotting of blood.

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Hemoglobin in the context of Iron oxide

An iron oxide is a chemical compound composed of iron and oxygen. Several iron oxides are recognized. Often they are non-stoichiometric. Ferric oxyhydroxides are a related class of compounds, perhaps the best known of which is rust.

Iron oxides and oxyhydroxides are widespread in nature and play an important role in many geological and biological processes. They are used as iron ores, pigments, catalysts, and in thermite, and occur in hemoglobin. Iron oxides are inexpensive and durable pigments in paints, coatings and colored concretes. Colors commonly available are in the "earthy" end of the yellow/orange/red/brown/black range. When used as a food coloring, it has E number E172.

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Hemoglobin in the context of Red blood cell

Red blood cells (RBCs), referred to as erythrocytes (from Ancient Greek erythros 'red' and kytos 'hollow vessel', with -cyte translated as 'cell' in modern usage) in academia and medical publishing, also known as red cells, erythroid cells, and rarely haematids, are the most common type of blood cell and the vertebrate's principal means of delivering oxygen (O2) to the body tissues—via blood flow through the circulatory system. Erythrocytes take up oxygen in the lungs, or in fish the gills, and release it into tissues while squeezing through the body's capillaries.

The cytoplasm of a red blood cell is rich in hemoglobin (Hb), an iron-containing biomolecule that can bind oxygen and is responsible for the red color of the cells and the blood. Each human red blood cell contains approximately 270 million hemoglobin molecules. The cell membrane is composed of proteins and lipids, and this structure provides properties essential for physiological cell function such as deformability and stability of the blood cell while traversing the circulatory system and specifically the capillary network.

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Hemoglobin in the context of Pallor

Pallor is a pale color of the skin that can be caused by illness, emotional shock or stress, stimulant use, or anemia, and is the result of a reduced amount of oxyhaemoglobin and may also be visible as pallor of the conjunctivae of the eyes on physical examination.

Pallor is more evident on the face and palms. It can develop suddenly or gradually, depending on the cause. It is not usually clinically significant unless it is accompanied by a general pallor (pale lips, tongue, palms, mouth and other regions with mucous membranes). It is distinguished from similar presentations such as hypopigmentation (lack or loss of skin pigment) or simply a lightly-melanated complexion.

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Hemoglobin in the context of Cyanotic

Cyanosis is the change of tissue color to a bluish-purple hue, as a result of decrease in the amount of oxygen bound to the hemoglobin in the red blood cells of the capillary bed. Cyanosis is apparent usually in the body tissues covered with thin skin, including the mucous membranes, lips, nail beds, and ear lobes. Some medications may cause discoloration such as medications containing amiodarone or silver. Furthermore, mongolian spots, large birthmarks, and the consumption of food products with blue or purple dyes can also result in the bluish skin tissue discoloration and may be mistaken for cyanosis. Appropriate physical examination and history taking is a crucial part to diagnose cyanosis. Management of cyanosis involves treating the main cause, as cyanosis is not a disease, but rather a symptom.

Cyanosis is further classified into central cyanosis and peripheral cyanosis.

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Hemoglobin in the context of Blood in stool

Blood in stool looks different depending on how early it enters the digestive tract—and thus how much digestive action it has been exposed to—and how much there is. The term can refer either to melena, with a black appearance, typically originating from upper gastrointestinal bleeding; or to hematochezia, with a red color, typically originating from lower gastrointestinal bleeding. Evaluation of the blood found in stool depends on its characteristics, in terms of color, quantity and other features, which can point to its source, but more serious conditions can present with a mixed picture, or with the form of bleeding that is found in another section of the tract. The term "blood in stool" is usually only used to describe visible blood, and not fecal occult blood, which is found only after physical examination and chemical laboratory testing.

In infants, the Apt test, a test that is particularly useful in cases where a newborn has blood in stool or vomit, can be used to distinguish fetal hemoglobin from maternal blood based on the differences in composition of fetal hemoglobin as compared to the hemoglobin found in adults. A non-harmful cause of neonatal bleeding include swallowed maternal blood during birth; However, serious causes include Necrotizing Enterocolitis (NEC), a severe inflammatory condition affecting premature infants, and midgut volvulus, a life-threatening twisting that requires emergency surgery.

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Hemoglobin in the context of Whole blood

Whole blood (WB) is human blood from a standard blood donation. It is used in the treatment of hemorrhagic shock, in exchange transfusion, and when people donate blood to themselves (autologous transfusion). One unit of whole blood (approximately 450 mL) increases hemoglobin levels by about 10 g/L. Cross matching is typically done before the blood is given. It is either given intravenously or through Intraosseous infusion.

Side effects include red blood cell breakdown, high blood potassium, infection, volume overload, lung injury, and allergic reactions such as anaphylaxis. Whole blood is made up of red blood cells, white blood cells, platelets, and blood plasma. It is best within a day of collection; however, it can be stored for up to three weeks if refrigerated (1-6 °C). The blood is typically combined with an anticoagulant and preservative during the collection process.

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Hemoglobin in the context of Blood transfusion

Blood transfusion is the process of transferring blood products into a person's circulation intravenously. Transfusions are used for various medical conditions to replace lost components of the blood. Early transfusions used whole blood, but modern medical practice commonly uses only components of the blood, such as red blood cells, plasma, platelets, and other clotting factors. White blood cells are transfused only in very rare circumstances, since granulocyte transfusion has limited applications. Whole blood has come back into use in the trauma setting.

Red blood cells (RBC) contain hemoglobin and supply the cells of the body with oxygen. White blood cells are not commonly used during transfusions, but they are part of the immune system and also fight infections. Plasma is the "yellowish" liquid part of blood, which acts as a buffer and contains proteins and other important substances needed for the body's overall health. Platelets are involved in blood clotting, preventing the body from bleeding. Before these components were known, doctors believed that blood was homogeneous. Because of this scientific misunderstanding, many patients died because of incompatible blood transferred to them.

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Hemoglobin in the context of Porphyria cutanea tarda

Porphyria cutanea tarda (PCT) is a form of long-term porphyria characterised by fragile skin and sore blisters in areas of skin that receive higher levels of exposure to sunlight, such as the face and backs of the hands. These blisters burst easily resulting in erosions, crusts, and superficial ulcers. There is often associated darkened skin color and extra facial hair growth. Healing is typically slow, leading to scarring and milia, while changes such as hair loss, and alterations in nails may also occur. A slightly purplish tint may be seen around the eyes. Scleroderma-like thick skin may develop over fingers, scalp, behind the ears, at the back of the neck, or in the front of the chest. The urine may appear dark. Unlike other porphyrias, PCT does not cause severe illness.

The disorder results from a deficiency of uroporphyrinogen III decarboxylase, used in the production of heme, a vital component of hemoglobin. It is generally divided into three types; familial, non-familial, and acquired. The condition can be related to liver disease and a history of excessive alcohol consumption. It is a recognised complication of hepatitis C. Other associated conditions include type 2 diabetes, metabolic syndrome, HIV, SLE, and haemochromatosis. Smoking, and the use of estrogen in males with prostate cancer and females on combined contraceptive pill may also trigger PCT. Renal dialysis may cause retention of porphyrins and cause PCT.

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Hemoglobin in the context of Emperor penguin

The emperor penguin (Aptenodytes forsteri) is the tallest and heaviest of all living penguin species and is endemic to Antarctica. The male and female are similar in plumage and size, reaching 100 cm (39 in) in length and weighing from 22 to 45 kg (49 to 99 lb). Feathers of the head and back are black and sharply delineated from the white belly, pale-yellow breast and bright-yellow ear patches.

Like all species of penguin, the emperor is flightless, with a streamlined body, and wings stiffened and flattened into flippers for a marine habitat. Its diet consists primarily of fish, but also includes crustaceans, such as krill, and cephalopods, such as squid. While hunting, the species can remain submerged around 20 minutes, diving to a depth of 535 m (1,755 ft). It has several adaptations to facilitate this, including an unusually structured haemoglobin to allow it to function at low oxygen levels, solid bones to reduce barotrauma, and the ability to reduce its metabolism and shut down non-essential organ functions.

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Hemoglobin in the context of Skin color

Human skin color ranges from the darkest brown to the lightest hues. Differences in skin color among individuals is caused by variation in pigmentation, which is largely the result of genetics (inherited from one's biological parents), and in adults in particular, due to exposure to the sun, disorders, or some combination thereof. Differences across populations evolved through natural selection and sexual selection, because of social norms and differences in environment, as well as regulation of the biochemical effects of ultraviolet radiation penetrating the skin.

Human skin color is influenced greatly by the amount of the pigment melanin present. Melanin is produced within the skin in cells called melanocytes; it is the main determinant of the skin color of darker-skin humans. The skin color of people with light skin is determined mainly by the bluish-white connective tissue under the dermis and by the hemoglobin circulating in the veins of the dermis. The red color underlying the skin becomes more visible, especially in the face, when, as a consequence of physical exercise, sexual arousal, or the stimulation of the nervous system (e.g. due to anger or embarrassment), arterioles dilate. Color is not entirely uniform across an individual's skin; for example, the skin of the palm and the soles of the feet is lighter than most other skin; this is more noticeable in darker-skinned people.

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Hemoglobin in the context of Myoglobin

Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. Myoglobin consists of non-polar amino acids at the core of the globulin, where the heme group is non-covalently bounded with the surrounding polypeptide of myoglobin. In humans, myoglobin is found in the bloodstream only after muscle injury.

High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A, and Type II B; although many older texts describe myoglobin as not found in smooth muscle, this has proved erroneous: there is also myoglobin in smooth muscle cells.

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Hemoglobin in the context of Spleen

The spleen (from Anglo-Norman espleen, ult. from Ancient Greek σπλήν, splḗn) is an organ found in almost all vertebrates. Similar in structure to a large lymph node, it acts primarily as a blood filter.

The spleen plays important roles in regard to red blood cells (erythrocytes) and the immune system. It removes old red blood cells and holds a reserve of blood, which can be valuable in case of hemorrhagic shock, and also recycles iron. As a part of the mononuclear phagocyte system, it metabolizes hemoglobin removed from senescent red blood cells. The spleen is a center of activity of the mononuclear phagocyte system and is analogous to a large lymph node, as its absence causes a predisposition to certain infections. The globin portion of hemoglobin is degraded to its constitutive amino acids, and the heme portion is metabolized to bilirubin, which is removed in the liver.

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Hemoglobin in the context of Anemia

Anemia (also spelt anaemia in British English) is a blood disorder in which the blood has a reduced ability to carry oxygen. This can be due to a lower than normal number of red blood cells, a reduction in the amount of hemoglobin available for oxygen transport, or abnormalities in hemoglobin that impair its function. The name is derived from Ancient Greek ἀν- (an-) 'not' and αἷμα (haima) 'blood'.

When anemia comes on slowly, the symptoms are often vague, such as tiredness, weakness, shortness of breath, headaches, and a reduced ability to exercise. When anemia is acute, symptoms may include confusion, feeling like one is going to pass out, loss of consciousness, and increased thirst. Anemia must be significant before a person becomes noticeably pale. Additional symptoms may occur depending on the underlying cause. Anemia can be temporary or long-term and can range from mild to severe.

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Hemoglobin in the context of Ligand (biochemistry)

In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from Latin ligare, which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformational isomerism (conformation) of the target protein. In DNA-ligand binding studies, the ligand can be a small molecule, ion, or protein which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure.

Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces. The association or docking is actually reversible through dissociation. Measurably irreversible covalent bonding between a ligand and target molecule is atypical in biological systems. In contrast to the definition of ligand in metalorganic and inorganic chemistry, in biochemistry it is ambiguous whether the ligand generally binds at a metal site, as is the case in hemoglobin. In general, the interpretation of ligand is contextual with regard to what sort of binding has been observed.

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