The role of haptoglobin in the clearance and distribution of extracorpuscular hemoglobin.
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منابع مشابه
Heterotropic Effect of β-lactam Antibiotics on Antioxidant Property of Haptoglobin) 2-2(-Hemoglobin Complex
Haptoglobin (Hp) is a mammalian serum glycoprotein showing a genetic polymorphism with three types, 1-1, 2-2 and 1-2. Hp appears to conserve the recycling of heme-iron by forming an essentially irreversible but non-covalent complex with hemoglobin which is released into the plasma by erythrocyte lysis. As an important consequence, Haptoglobin-Hemoglobin complex (Hp-Hb) shows considerable antiox...
متن کاملHeterotropic Effect of β-lactam Antibiotics on Antioxidant Property of Haptoglobin) 2-2(-Hemoglobin Complex
Haptoglobin (Hp) is a mammalian serum glycoprotein showing a genetic polymorphism with three types, 1-1, 2-2 and 1-2. Hp appears to conserve the recycling of heme-iron by forming an essentially irreversible but non-covalent complex with hemoglobin which is released into the plasma by erythrocyte lysis. As an important consequence, Haptoglobin-Hemoglobin complex (Hp-Hb) shows considerable antiox...
متن کاملThe glomerular clearance and renal transport of hemoglobin in adult males.
The demonstration by Polonovski, Jayle, Boussier and Badin (1, 2) that certain plasma proteins have the property of binding extracorpuscular hemoglobin has led to recent re-evaluation of the mechanisms of renal transport of hemoglobin in the dog (3) and in man (4). Lathem (4) showed that circulating extracorpuscular hemoglobin is bound quantitatively to the a2-globulin, haptoglobin. By utilizin...
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Background: Haptoglobin (Hp) is a plasma α2-sialoglycoprotein that contains alpha and beta chains. It displays in three common phenotypes, Hp1-1, Hp2-1, and Hp2-2. Proteins expressed by polymorphic genes have grossly different molecular sizes resulting in different diffusion rates in the brain. Haptoglobin expressed by the Hp2-2 genotype has lower hemoglobin-binding capacity than Hp1-1 or...
متن کاملBinding of acellular, native and cross-linked human hemoglobins to haptoglobin: enhanced distribution and clearance in the rat.
It is well established that hemoglobin resulting from red cell lysis binds to haptoglobin in plasma to form a complex. The increased molecular size precludes its filtration by the kidneys, redirecting it toward hepatocellular entry. Chemically cross-linked hemoglobins are designed to be resistant to renal excretion, even in the absence of haptoglobin. The manner in which binding to haptoglobin ...
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عنوان ژورنال:
- Blood
دوره 17 شماره
صفحات -
تاریخ انتشار 1961