The changes of the structure and content of the erythrocyte membrane band 3 protein and its function of anion transport and blood gases inside and out of the erythrocytes were observed under isobaric hypoxia and hypox...The changes of the structure and content of the erythrocyte membrane band 3 protein and its function of anion transport and blood gases inside and out of the erythrocytes were observed under isobaric hypoxia and hypoxia-hypercapnia in rats. It was found t展开更多
Band 3, serving as an anion transporter, is the most abundant protein in the humanerythrocyte plasma membrane. It has two strucurally and functionally distinct domains.The membrane domain is responsible for the anion ...Band 3, serving as an anion transporter, is the most abundant protein in the humanerythrocyte plasma membrane. It has two strucurally and functionally distinct domains.The membrane domain is responsible for the anion exchange activity, while thecytoplasmic domain of Band 3 binds with components of the cytoskeleton (such asankyrin) to stabilize the cytoskeleton network. Although the cytoplasmic domain is展开更多
Band 3 and glucose transport protein (GluTl) are two kinds of important proteins in the human erythro-cyte membranes. Bis(sulfosuccinimidyl)suberate (BS ), an impermeable cross-linker of band 3, inhibited NO2- transpo...Band 3 and glucose transport protein (GluTl) are two kinds of important proteins in the human erythro-cyte membranes. Bis(sulfosuccinimidyl)suberate (BS ), an impermeable cross-linker of band 3, inhibited NO2- transport, showing that anion exchange is affected by the association state of band 3 in the intact erythrocyte membranes. At the same time, the rates of glucose transport of both exit and entry declined. The amount of monomers of band 3 was decreased after treatment of the erythrocytes with BS3, but there was no change in GluTl according to the SDS-PAGE patterns. This demonstrates that band 3 and GluTl would be linkaged together in the erythrocyte membranes for the requirement of rapid and cooperative performance of physiological functions of the membrane proteins.展开更多
文摘The changes of the structure and content of the erythrocyte membrane band 3 protein and its function of anion transport and blood gases inside and out of the erythrocytes were observed under isobaric hypoxia and hypoxia-hypercapnia in rats. It was found t
基金Department of Protein Engineering, Institute of Biophysics, the Chinese Academy of Sciences, Beijing 10010, China.
文摘Band 3, serving as an anion transporter, is the most abundant protein in the humanerythrocyte plasma membrane. It has two strucurally and functionally distinct domains.The membrane domain is responsible for the anion exchange activity, while thecytoplasmic domain of Band 3 binds with components of the cytoskeleton (such asankyrin) to stabilize the cytoskeleton network. Although the cytoplasmic domain is
基金This work was supported by the National Natural Science Foundation of China (Grant Nos. 30070205and 39730150)
文摘Band 3 and glucose transport protein (GluTl) are two kinds of important proteins in the human erythro-cyte membranes. Bis(sulfosuccinimidyl)suberate (BS ), an impermeable cross-linker of band 3, inhibited NO2- transport, showing that anion exchange is affected by the association state of band 3 in the intact erythrocyte membranes. At the same time, the rates of glucose transport of both exit and entry declined. The amount of monomers of band 3 was decreased after treatment of the erythrocytes with BS3, but there was no change in GluTl according to the SDS-PAGE patterns. This demonstrates that band 3 and GluTl would be linkaged together in the erythrocyte membranes for the requirement of rapid and cooperative performance of physiological functions of the membrane proteins.
