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Effect on membrane transport in the erythrocytes by band 3 cross-linking
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作者 Weihua Jiang Yu Ding +3 位作者 Xiaojian Hu Feng Peng Hanqing Zhou Zhihong Zhang 《Chinese Science Bulletin》 SCIE EI CAS 2002年第22期1889-1892,共4页
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
关键词 bis(sulfosuccinimidyl)suberate (bs^3) BAND 3 GLUCOSE transporter.
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