Salhany J M, Rauenbuehler P B, Sloan R L
Biochem Biophys Res Commun. 1987 Mar 30;143(3):959-64. doi: 10.1016/0006-291x(87)90344-5.
Pyridoxal-5'-phosphate is known to label the two integral, chymotryptic domains (CH17 and CH35) of the erythrocyte anion exchange protein known as band 3. The CH35 sites are mutually exclusive with stilbene disulfonate binding, while the CH17 sites are not. Selective, irreversible pyridoxal-5'-phosphate labeling of CH17, reduces the transport inhibitory potency due to reversible stilbene disulfonate binding to vacant, nonoverlapping CH35 sites. We conclude that multisite allosteric interactions can occur on one band 3 monomer.
已知磷酸吡哆醛可标记红细胞阴离子交换蛋白（即带3蛋白）的两个完整的胰凝乳蛋白酶敏感结构域（CH17和CH35）。CH35位点与二苯乙烯二磺酸盐结合相互排斥，而CH17位点则不然。对CH17进行选择性、不可逆的磷酸吡哆醛标记，会降低由于二苯乙烯二磺酸盐可逆结合到空的、不重叠的CH35位点而产生的转运抑制效力。我们得出结论，多位点变构相互作用可在一个带3单体上发生。
