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+.-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.