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Tissue Engineering and Application in Tropical Medicine
Published in Rajesh K. Kesharwani, Raj K. Keservani, Anil K. Sharma, Tissue Engineering, 2022
Thalassemia is an important hemoglobin disorder. The basic pathophysiology is the genetic defect that results in abnormal globin synthesis. At present, thalassemia is common in several tropical countries, especially for tropical Southeast Asia. The bone defect and hepatosplenomegaly are common sequel in thalassemia. Many patients require transfusion therapy for correction of anemic problem. The risk of this transfusion treatment is well known. The iron overload is a common complication in the patient with polytransfusion and requires iron chelation therapy. At present, the gold standard for the effective treatment of thalassemia is stem cell therapy. Hence, the role of tissue engineering for management of thalassemia is confirmed (Felfly and Haddad, 2014). Many studies are in development and trial phases. The good examples are on the management of thalassemia-related wound. Afradi et al. (2017) reported on the use of tissue engineering technology in treatment of 100 chronic thalassemic leg wounds by plasma-rich platelets. Afradi et al. (2017) reported using new platelet-rich plasma (PRP) gel consisting of cytokines, growth factors, chemokines, and a fibrin scaffold derived from a patient’s blood and noted that the technique was useful in wound management in thalassemic patient.
Toxic Responses of the Blood
Published in Stephen K. Hall, Joana Chakraborty, Randall J. Ruch, Chemical Exposure and Toxic Responses, 2020
Hemoglobin is the oxygen-carrying protein of the red blood cells. The globin, or protein chains, has irregularly folded conformations that enclose the heme group in a hydrophobic pocket that forms the oxygen binding site. The active site of the heme group is a Fe2+ ion situated in a porphyrin ring. Of the two remaining coordination bonds, one is associated with an imidazole residue from the globin chain and the remaining bond is available for reversible binding with oxygen. No ligand is known to occupy this latter site in the case of deoxyhemoglobin. The reversible binding of oxygen by hemoglobin is called oxygenation. Four oxygen molecules bind to a hemoglobin. When the hemoglobin molecule is fully saturated, all four oxygen molecules are thought to be equivalent, and any one of them may be the first to be released. The release of the first oxygen, however, will greatly facilitate the release of the second oxygen molecule. In the same manner, the release of the second oxygen facilitates the release of the third oxygen. Release of the fourth oxygen does not occur under normal physiologic conditions.
Toxicology
Published in Martin B., S.Z., of Industrial Hygiene, 2018
Hemoglobin is the oxygen-carrying protein of the red blood cells. The globin, or protein chains, has irregularly folded conformations that enclose the heme group in a hydrophobic pocket that forms the oxygen binding site. The active site of the heme group is an Fe2+ ion situated in a porphyrin ring. The reversible binding of oxygen by hemoglobin is called oxygenation. When the hemoglobin molecule is fully saturated, all four oxygen molecules are thought to be equivalent, and any one of them may be the first to be released. The release of the first oxygen, however, will greatly facilitate the release of the second oxygen molecule. In the same manner, the release of the second oxygen facilitates the release of the third oxygen. Release of the fourth oxygen does not occur under normal physiologic conditions.
Analysis of coronavirus envelope protein with cellular automata model
Published in International Journal of Parallel, Emergent and Distributed Systems, 2022
Raju Hazari, Parimal Pal Chaudhuri
The hypothesis has been validated from mutational study on two proteins: (i) HBB beta-globin hemoglobin protein [3,36,37], (ii) mutations reported in COVID-2 infected patients [9,36]. For each of these case studies, difference of CAML model parameter between wild and mutant corroborates the results reported in vitro/in vivo studies in respect of deviation of structure–function of specific mutant from its wild leading to a specific disease.