Unlike its human counterpart, band 3 anion exchange protein from goat erythrocyte membrane shows a lack of reactivity against various -SH oxidants and protease treatments.
Studies involving a number of -SH oxidants and proteases were made to analyse the organization of band 3 in goat erythrocyte membrane. -SH oxidizing agents such as diamide, Cu2+.o-phenanthroline and phenylene dimaleimide, known to cause cross-linking of human erythrocyte band 3, failed to show any cross-linking in the case of goat band 3 protein. When resolved to their individual components using -SH reducing agent beta-mercaptoethanol, high molecular weight protein adducts formed as a result of diamide treatment did not show any band 3 on two-dimensional electrophoresis. Also no proteolysis of band 3 was detected when intact goat erythrocytes were exposed to pronase, though marked proteolysis was noticed in the case of human band 3 proteins under similar conditions. These studies involving -SH oxidant and protease treatments suggest a different organization for goat erythrocyte band 3 protein as compared to that of human in erythrocyte membrane.
Khan
M T
MT
Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, India.
Saleemuddin
M
M
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry* / Q000187:drug effects; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D015180:Electrophoresis, Gel, Two-Dimensional; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006041:Goats / Q000097:blood*; D006801:Humans; D008970:Molecular Weight; D011402:Pronase / Q000494:pharmacology*; D013045:Species Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology*
D001457:Anion Exchange Protein 1, Erythrocyte; D003432:Cross-Linking Reagents; D013439:Sulfhydryl Reagents; D011402:Pronase