Williamson F A, Morré D J, Shen-Miller J
Cell Tissue Res. 1976 Aug 10;170(4):477-84. doi: 10.1007/BF00361705.
5'-Nucleotidase activity of rat liver plasma membrane is markedly inhibited by concanavalin A. Taken together with a unilateral pattern of labelling of concanavalin A binding sites with hemocyanin, the results indicate that an allosteric site of the enzyme is at the outer surface of the membrane.
伴刀豆球蛋白A可显著抑制大鼠肝细胞膜的5'-核苷酸酶活性。结合伴刀豆球蛋白A结合位点用血蓝蛋白进行单侧标记的模式,结果表明该酶的别构位点位于膜的外表面。