Jayoti Vidyapeeth Woman’s University, Jaipur
A review article on oxygen binding to hemoglobin
• Sonali (jv-d/17/1341)
• Manisha Raha (jv-d /17/1353)
• Juhi kumari (jv’n-d/17/1354)
Dmlt (2nd semi)
Over the year’s study of the disorders of hemoglobin has served as a paradigm for gaining insights into the cellular and molecular biology as well as the path physiology.
Non enzymatic glycerin increases hemoglobin-oxygen affinity and reduce oxygen delivery to tissues by altering the structure and function of hemoglobin the review address the strengths and weakness of each of these tests and gives advice on their clinical use the clinical relevance of the hemoglobin-oxygen dissociation curve will be reviewed and we will show how a mathematical model of the curve. The long term genetically coded adaptations in oxygen transport encountered in animals that permanently are subjected to low environmental o2 tensions commonly result from changes in the molecular structure of hemoglobin.
• Hemoglobin comprise four Goblin chain, each containing hem molecule which reversibly bind
• Sao2 ( stand of peripheral oxygen )
• Po2 ( partial pressure of oxygen )
• Sao2( standard for peripheral capillary )
Ox hemoglobin is from during physiological respiration when oxygen binds to the hemoglobin component of hemoglobin in red blood cell this process occurs in the pulmonary capillaries adjacent to the alveoli of the lungs. The oxygen then travels through the blood stream to the cells where it is utilized in glycol-sis and in the production of ATP by the process of oxidative phosphorylation.
Hemoglobin molecule also bind to competitive inhibitors such as carbon monoxide and allosteric legends such as nitric oxide bind to specific trial group in the globin protein to form an s-nitrosothiol which dissociates into free nitric oxide from its hemi site.
The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecular with the first oxygen bound influencing the shape of the binding sites for the next oxygen in way favorable for binding. The positive cooperative binding is achieved through strict conformational changes of the hemoglobin protein complex. When one subunit protein in hemoglobin becomes oxygenated a conformational or structural change in the whole complex is initiated causing the other subunits to gain an increased affinity for oxygen. Hence, the oxygen binding curve of hemoglobin is sigmoidal, or s-shaped, as opposed to the normal hyperbolic curve associated with noncoprative binding.
Arterial oxygen saturation and (sao2) and partial pressure of oxygen(po2) were determined with simultaneous monitoring of spo2 in 261 type 2 diabetic patients during ventilation the common earthworm L terrestris was purchased from Carolina biological supply co (Burlington,Nc).The supernatant was then centrifuged at 150,000x g 2hr at 4 degrees Celsius. Hemoglobin concentration was determined with a model t-890 counter. Blood hba1c concentration was assayed using ion-exchange liquid chromatography with bio-red variant hemoglobin testing system.
Hemoglobin is a support base for all life process. Elevated blood HbA1c levels lead to and overestimation of sao2 by spo2 suggesting that arterial blood gas analysis .In the normal physiological conditions it is salutary under stress the nature that promotes cell health is disrupted leading to real threat . Many abnormalities in hemoglobin exist a can be to altered structure and production of globing chains the binding of other legends, or an abnormal hem –iron complex.
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