Haemoglobin in the context of Inorganic ions


Haemoglobin in the context of Inorganic ions

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⭐ Core Definition: Haemoglobin

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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👉 Haemoglobin in the context of Inorganic ions

Inorganic ions in animals and plants are ions necessary for vital cellular activity. In body tissues, ions are also known as electrolytes, essential for the electrical activity needed to support muscle contractions and neuron activation. They contribute to osmotic pressure of body fluids as well as performing a number of other important functions. Below is a list of some of the most important ions for living things as well as examples of their functions:

  • Ca – calcium ions are a component of bones and teeth. They also function as biological messengers, as do most of the ions listed below. (See Hypocalcaemia.)
  • Zn - zinc ions are found in very small concentrations in the body, and their main purpose is that of an antioxidant; the zinc ions act as antioxidants both generally and for liver specific pro-oxidants. Zinc ions can also act as an antioxidant-like stabilizer for some macro-molecules which bind zinc ions with high affinity, especially in cysteine-rich binding sites. These binding sites use these zinc ions as a stabilizer to protein folds, making these protein motifs more rigid in structure. These structures include zinc fingers, and have several different conformations.
  • K – potassium ions' main function in animals is osmotic balance, particularly in the kidneys. (See Hypokalemia.)
  • Na – sodium ions have a similar role to potassium ions. (See Sodium deficiency.)
  • Mn- manganese ions are seen being used as stabilizer for varying protein configurations. However, manganese ion overexposure is linked to several neurodegenerative diseases such as Parkinson's disease.
  • Mg – magnesium ions are a component of chlorophyll. (See Magnesium deficiency (plants))
  • Cl – inability to transport chloride ions in humans manifests itself as cystic fibrosis (CF)
  • CO
    3
     – the shells of sea creatures are calcium carbonate. In blood approximately 85% of carbon dioxide, is converted into aqueous carbonate ions (an acidic solution), allowing a greater rate of transportation.
  • Co- cobalt ions are present in the human body in amounts from 1 to 2 mg. Cobalt is observed in the heart, liver, kidney, and spleen, and considerably smaller quantities in the pancreas, brain, and serum. Cobalt is a necessary component of vitamin B12 and a fundamental coenzyme of cell mitosis. Cobalt is crucial for amino acid formation and some proteins to create myelin sheath in nerve cells. Cobalt also plays a role in creating neurotransmitters, which are vital for proper function within the organism.
  • PO
    4
     – adenosine triphosphate (ATP) is a common molecule which stores energy in an accessible form. Bone is calcium phosphate.
  • Fe/Fe – as found in haemoglobin, the main oxygen carrying molecule has a central iron ion.
  • NO
    3
     – source of nitrogen in plants for the synthesis of proteins.
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Haemoglobin in the context of Max Perutz

Max Ferdinand Perutz OM CH CBE FRS (19 May 1914 – 6 February 2002) was an Austrian-born British molecular biologist, who shared the 1962 Nobel Prize for Chemistry with John Kendrew, for their studies of the structures of haemoglobin and myoglobin. He went on to win the Royal Medal of the Royal Society in 1971 and the Copley Medal in 1979. At Cambridge he founded and chaired (1962–79) The MRC Laboratory of Molecular Biology (LMB), fourteen of whose scientists have won Nobel Prizes.

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Haemoglobin in the context of Bacillus anthracis

Bacillus anthracis is a gram-positive and rod-shaped bacterium that causes anthrax, a deadly disease to livestock and, occasionally, to humans. It is the only permanent (obligate) pathogen within the genus Bacillus. Its infection is a type of zoonosis, as it is transmitted from animals to humans. It was discovered by a German physician Robert Koch in 1876, and became the first bacterium to be experimentally shown as a pathogen. The discovery was also the first scientific evidence for the germ theory of diseases.

B. anthracis measures about 3 to 5 μm long and 1 to 1.2 μm wide. The reference genome consists of a 5,227,419 bp circular chromosome and two extrachromosomal DNA plasmids, pXO1 and pXO2, of 181,677 and 94,830 bp respectively, which are responsible for the pathogenicity. It forms a protective layer called endospore by which it can remain inactive for many years and suddenly becomes infective under suitable environmental conditions. Because of the resilience of the endospore, the bacterium is one of the most popular biological weapons. The protein capsule (poly-D-gamma-glutamic acid) is key to evasion of the immune response. It feeds on the heme of blood protein haemoglobin using two secretory siderophore proteins, IsdX1 and IsdX2.

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Haemoglobin in the context of Chromoprotein

A chromoprotein is a conjugated protein that contains a pigmented prosthetic group (or cofactor). A common example is haemoglobin, which contains a heme cofactor, which is the iron-containing molecule that makes oxygenated blood appear red. Other examples of chromoproteins include other hemochromes, cytochromes, phytochromes and flavoproteins.

In hemoglobin there exists a chromoprotein (tetramer MW:4 x 16.125 =64.500), namely heme, consisting of Fe++ four pyrrol rings.

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Haemoglobin in the context of Arterial blood

Arterial blood is the oxygenated blood in the circulatory system found in the pulmonary vein, the left chambers of the heart, and in the arteries. It is bright red in color, while venous blood is dark red in color (but looks purple through the translucent skin). It is the contralateral term to venous blood.

Framed in the cardiac cycle, often historically accredited to the Wiggers diagram, arterial blood has just passed through the lungs and is ready to boost oxygen to sustain the peripheral organs. The essential difference between venous and arterial blood is the curve of the oxygen saturation of haemoglobin. The difference in the oxygen content of the blood between the arterial blood and the venous blood is known as the arteriovenous oxygen difference.

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Haemoglobin in the context of Urine test strip

A urine test strip or dipstick is a basic diagnostic tool used to determine pathological changes in a patient's urine in standard urinalysis.

A standard urine test strip may comprise up to 10 different chemical pads or reagents which react (change color) when immersed in, and then removed from, a urine sample. The test can often be read in as little as 60 to 120 seconds after dipping, although certain tests require longer. Routine testing of the urine with multiparameter strips is the first step in the diagnosis of a wide range of diseases. The analysis includes testing for the presence of proteins, glucose, ketones, haemoglobin, bilirubin, urobilinogen, acetone, nitrite and leucocytes as well as testing of pH and specific gravity or to test for infection by different pathogens.

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Haemoglobin in the context of Plasma protein


Plasma proteins, sometimes referred to as blood proteins, are proteins present in blood plasma. They perform many different functions, including transport of hormones, vitamins and minerals in activity and functioning of the immune system. Other blood proteins act as enzymes, complement, components, protease inhibitors or kinin precursors. Contrary to popular belief, haemoglobin is not a blood protein, as it is carried within red blood cells, rather than in the blood serum.

Serum albumin accounts for 55% of blood proteins, is a major contributor to maintaining the oncotic pressure of plasma and assists, as a carrier, in the transport of lipids and steroid hormones. Globulins make up 38% of blood proteins and transport ions, hormones, and lipids assisting in immune function. Fibrinogen comprises 7% of blood proteins; conversion of fibrinogen to insoluble fibrin is essential for blood clotting. The remainder of the plasma proteins (1%) are regulatory proteins, such as enzymes, proenzymes, and hormones. All blood proteins are synthesized in liver except for the gamma globulins.

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Haemoglobin in the context of Sickle-cell disease

Sickle cell disease (SCD), also simply called sickle cell, is a group of inherited haemoglobin-related blood disorders. The most common type is known as sickle cell anemia. Sickle cell anemia results in an abnormality in the oxygen-carrying protein haemoglobin found in red blood cells. This leads to the red blood cells adopting an abnormal sickle-like shape under certain circumstances. With this shape, they are unable to deform as they pass through capillaries, causing blockages.

Problems in sickle cell disease typically begin around 5 to 6 months of age. Several health problems may develop, such as attacks of pain (known as a sickle cell crisis) in joints, anemia, swelling in the hands and feet, bacterial infections, dizziness and stroke. The probability of severe symptoms, including long-term pain, increases with age. Without treatment, people with sickle cell disease rarely reach adulthood, but with good healthcare, median life expectancy is between 58 and 66 years. All of the major organs are affected by sickle cell disease. The liver, heart, kidneys, lungs, gallbladder, eyes, bones, and joints can be damaged from the abnormal functions of the sickle cells and their inability to effectively flow through the small blood vessels.

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