Hemoglobin is a metalloprotein that conveys oxygen [1] from lungs to the peripheral tissues such as muscles, liver and intestines. Human adult hemoglobin (Hb) is a tetrameric blood protein, consisting of two pairs of and β polypeptide chains. The hemoglobin tetramer contains a total of 6 Tryptophanes. The intrinsic fluorescence of Hb originates mainly from a Trp residue located near to the heme moiety. Methotrexate, a well-known inhibitor of dihydrofolate reductase [2] an enzyme which inhibits the synthesis of new DNA, was widely used in the treatment of various cancers.
Since 1985, MTX has been used as an effective drug in rheumatoid arthritis [3][4][5], psoriasis [6][7], acute lymphoblastic leukemia [8] lymphoma, head and neck cancer [9], breast cancer [10] and osteosarcoma [11]. Additionally, MTX-conjugated AuNPs distinguished by cytotoxic effects on human choriocarcinoma cells [12] and MTX liposome were used as oral drug delivery carriers [13].
A LC-MS/MS based method was recently used to estimate MTX polyglutamate concentration in the red blood cell [14]. Recent spectroscopic studies reveal the interaction of MTX with nucleic acids [15] or serum albumin [16].
Various spectroscopic methods have been used to study the interaction of small organic molecules with proteins. Several studies reveal the interaction of flavonoids [17][18][19], dyes [20][21][22], allosteric effectors [23] or other organic compounds [24][25] with hemoglobin.
Moreover, some studies focused on interaction of various antibiotics as oxytetracycline [26], chloramphenicol [27] and cephalosporines [28] with hemoglobin:
In particularly, hemoglobin interacts with several drugs: docetaxel [29], alprazolam-a sedative and antidepressant drug [30], tramo...
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...anda, and P. Karmakar, “Alprazolam induced conformational change in hemoglobin.,” Int. J. Biol. Macromol., vol. 41, no. 1, pp. 23–9, Jun. 2007.
[31] S. Tunç, A. Cetinkaya, and O. Duman, “Spectroscopic investigations of the interactions of tramadol hydrochloride and 5-azacytidine drugs with human serum albumin and human hemoglobin proteins.,” J. Photochem. Photobiol. B., vol. 120, pp. 59–65, Mar. 2013.
[32] J. R. Lakowicz, “Principles of Fluorescence Spectroscopy BT - Principles of Fluorescence Spectroscopy,” in Princ. Fluoresc. Spectrosc., Springer New York, 2006, p. 954.
[33] G. M. Artmann, L. Burns, J. M. Canaves, A. Temiz-Artmann, G. W. Schmid-Schönbein, S. Chien, and C. Maggakis-Kelemen, “Circular dichroism spectra of human hemoglobin reveal a reversible structural transition at body temperature.,” Eur. Biophys. J. EBJ, vol. 33, no. 6, pp. 490–496, 2004.
Hemoglobin is composed of four subunits (beta/Alpha) containing a heme group which binds an iron and that iron binds to the oxygen. The blueness of the skin occurs when, rather than carrying oxygenated hemoglobin, our blood carries deoxygenated hemoglobin in increased amounts “>5 g/dL”. In this case, the baby is experiencing central cyanosis, which is abnormal and needs to be treated immediately. When the doctor attempted to give the baby oxygen via nasal cannula, it did not change the blood oxygen saturation because although the concentration of blood oxygen levels increased, there is too much deoxyhemoglobin to cause the blood oxygen saturation percent to increase back to its normal state. Cyanosis occurs either because of decrease of oxygen in the blood, or due to a congenital heart defect known
... to demonstrate that hemoglobin attaches to the VIVO2+ ion at two locations of comparable strengths, named β and γ. This study has also proven that the interaction of red blood cells cannot be ignored when the conveyance or the pharmacological properties of a V compound is taken into consideration. In general, this paper does well in supporting the information available concerning hemoglobin. This article boosts the information available, concerning the diseases, genetics and functions of hemoglobin proteins. The authors achieve this by getting down to the basic level via the examination of the crystallographic structures of hemoglobin. This research has demonstrated novel examples associated with hemoglobin, pertaining to its processes and its purpose of movement. This study has immense implications for the grasp and the management of various diseases of hemoglobin
Hematology is the study of structure, function and pathological disorders in the blood. Blood consists of 55% plasma and 45% blood cells. Plasma is a mixture of 7% protein, 91% water and 2% other solutes. The types of proteins present in blood are albumin, globulin, and fibrinogen. Other remaining solutes consist of ions, nutrients, gases and respiratory substances and waste products. On the other hand, 250 to 400 thousand pla...
The diminished rate of synthesis amongst the globin chains was first described from Cooley and Lee. However, the term “Thalassemia: was coined by Whipple and Bradford in 1936 (Bain, 2006). The term “Thalassemia” is derived from the Greek words “Thalassa” (sea) and “Heama” (blood) and refers to disorders associated with defective synthesis of the alpha or beta globin subunits of the hemoglobin molecule. Hemoglobin A (a2B2) is inherited. ...
Hemoglobin is an important feature in red blood cells, it attracts oxygen so the cell can perform its job. Because the cell has no DNA or RNA, it cannot be targeted but viruses.
Thalassemia also known as Cooley’s anemia (Catlin 2003) was originally described by Thomas Cooley in 1925 (Starr 2012). The name Thalassemia came from the Greek name for sea (thalassa). This was due to the fact that for many years, those who had been most affected lived in the vicinity of the Mediterranean Sea (Starr 2012). Beta thalassemia occurs most frequently in people from Mediterranean countries, North Africa, the Middle East, India, Central Asia, and Southeast Asia. Thalassemia is a genetic blood disorder that is inherited from parents. The absence or reduction in the production of hemoglobin is the cause of thalassemia. Hemoglobin is in the red blood cells, it is a protein that carries oxygen to cells throughout the body (Catlin 2011)). Thalassemia is characterized by quantitative defects in the synthesis of either the alpha hemoglobin for Alpha Thalassemia or the beta hemoglobin for Beta Thalassemia (Starr, 2012). It is not widely known how many people are affected by Thalassemia but the US populatio...
Each red blood cell in the human body contains about 280 million hemoglobin molecules. Hemoglobin is the most important component of red blood cells. Red blood cells are composed of a protein (globulin) and a molecule (heme), which binds to iron. Normal hemoglobin causes regular oxygen and carbon dioxide exchange. In the lungs, the heme, which binds to iron, component takes up oxygen and releases carbon dioxide. The red blood cells carry the oxygen to the body's tissues, where ...
"Ultraviolet/Visible Spectroscopy (UV-Vis)." YouTube. Royal Society of Chemistry, 28 Sept. 2008. Web. 26 Jan. 2014. .
Sickle cell anemia is the most common in hemoglobin mutation diseases due to mutation to beta-blobin gene. The substitution of valine for glutamate at position 6 of the beta chains paces a nonpolar residue on the outside of hemoglobin S. the oxygen affinity and allosteric properties of hemoglubin are virtually unaffected by this changes. However, this alternation markedly reduces the solubility of the deoxygenated but not the oxygenated form of hemoglobin. Thus, sicking occurs when there is a high concentration of the deoxygenated form of hemoglobin.
The study of structure, function and pathological disorders in blood is called “Haematology”. Blood consists of 55% plasma and 45% blood cells. Plasma is a mixture of 7% protein, 91% water and 2% other solutes. The types of proteins present in blood are albumin, globulin, and fibrinogen. Other remaining solutes consist of ions, nutrients, gases and respiratory substances and waste products. On th...
Sickle cell anemia is a blood disorder that affects hemoglobin (pronounced: hee-muh-glow-bin), a protein found in red blood cells that helps carry oxygen throughout the body.
I used the article titled, “The Reaction of Oxy Hemoglobin with Nitrite: Mechanism, Antioxidant-Modulated Effect, and Implications for Blood Substitute Evaluation” from the journal Molecules.
...r is hard to cure due to its ability to metastasis and avoid apoptosis due to mutation occurs in the genes during mitosis, especially on oncogen and tumour suppressor gene. Oncogen contribute to cancer cells by encouraging cells to grow and divide excessively while tumour suppressor genes inhibit apoptosis. As all cells on Earth require oxygen, nutrients and the ability to remove waste products to survive and develop, it seems possible to develop anti-cancer drugs which will target at those blood vessels which supply nutrients to tumour cells. Even though this method is providing some promising results, there is no significant improvement in the overall survival of the organism in the long term. Nevertheless, the understanding of cellular basis of cancer cells gain from numerous researches have certainly help in developing new and effective treatment for cancer.
Yonezawa, K, Hokkaido Igaku Zasshi, “Effect of blood hemoglobin on concentration on anaerobic threshold.” July 1991; 66(4): pages 458-67.
Thalassemia is a blood disorder transferred through families. It occurs when the body makes less hemoglobin than needed or an unusual form of hemoglobin. Hemoglobin is the protein in red blood cells that carry oxygen. The disorder makes an excessive amount of destruction of red blood cells. This eventually leads to anemia.