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Haptoglobin and free hemoglobin

Combined into a composite, showing a new antigenic determinants, the mononuclear cells, the hemoglobin of the surface of the macrophage Clear recognizes and binds receptor (CD163), after being swallowed degradation to the removed blood circulation free hemoglobin. This physiological phenomenon, a very interesting reference for clinical laboratory science indicators. When doctors experimental instrument found that the serum binding globin decreased, combined with the patient's clinical manifestations, can determine whether an intravascular hemolytic disease, such as paroxysmal nocturnal hemoglobinuria and favism, and congenital absence beads albumin. There are some other types of intravascular hemolysis and extravascular hemolysis haptoglobin can be reduced, the degree of reduction in regular and the severity of the disease of the same.



Haptoglobin main function is to form a stable complex, and then combined with the free hemoglobin mononuclear - macrophage system disposed. Under normal circumstances, the human red blood cells in the circulating blood, despite continuing subject to mechanical damage, but still maintain its integrity, with the erythrocytes having a good plasticity of the cell morphology and blood micro-environment is relatively stable. Some reason induced red blood cells in the blood vessel destruction, a large number of hemoglobin released into the blood circulation, the hemoglobin from human kidney filtration, cause kidney damage, and even cause irreversible renal damage. Haptoglobin and free hemoglobin combine to form a stable complex, due to its large molecular size, can not be excreted from the kidney, which can prevent the hemoglobin from glomerular filtration to avoid the damage of free hemoglobin in the renal tubules.


Combined the globin (haptoglobin, HP)

Also known as haptoglobin, with a molecular weight of 85,000 acid glycoprotein, widely present in the serum and other body fluids of humans and a variety of mammals. CAM electrophoresis and agarose gel electrophoresis, haptoglobin in α2 zones, in the molecule, there are two pairs of peptide chain (α chain and β chain) together form α2β2 tetramer. Haptoglobin primarily synthesized in the liver, its degradation also liver, the half-life of about 3.5 to 4 days.


Xanthine oxidase activity sites

The Mo atom of the molybdenum pterin cofactor addition with a terminal oxygen, a plurality of sulfur atom and connected to a terminal hydroxyl group. Xanthine to uric acid in the reaction, the oxygen on the molybdenum first transferred to the xanthine molecule, and then, the water molecules and the reactive intermediates undergo addition, so that the activity of the molybdenum center regeneration.
Molybdenum oxide with other known enzymes of the same, the product of the newly introduced oxygen atom is the oxygen from the water molecule, rather than oxygen molecules.


Xanthine oxidase traits

1 the appearance of a pale yellow liquid, based crystals suspended in 2.3 mol / L ammonium sulfate, l0mmol / L sodium phosphate buffer solution, containing 1mmol / L EDTA, 1mmol / L sodium salicylate, pH value of approximately 7.8, is iron - molybdenum flavoprotein.
2 can be oxidized hypoxanthine, xanthine, and aldehydes, and the like; the optimum pH value of 8.2, an isoelectric point of 5.3 to 5.4.
3. Activator is oxygen; inhibitors metal ions, cyanides, aldehydes, allopurinol, phosphates, imidazole, sodium chloride and potassium chloride.
4. Crude enzyme can be stored at 2 ℃ weeks vitality without reducing; freezing conditions can be stored for a long.