Evidence for two forms of ligandin (YaYa dimers of glutathione S-transferase) in rat liver and kidney.
Evidence for two forms of ligandin (YaYa dimers of glutathione S-transferase) in rat liver and kidney.
复制标题
大鼠肝脏和肾脏中存在两种形式配体蛋白（谷胱甘肽 S-转移酶 YaYa 二聚体）的证据。
作者：
D. Sheehan;T. Mantle
大鼠肝和肾胞质溶胶在pH 6下的CM-纤维素层析显示，除了最近描述的GST-YaYa（GST-L;我们的命名法）外，还存在谷胱甘肽S-转移酶（GST-F）的第二个Ya-亚基二聚体[Hayes和克拉克森（1982）生物化学杂志207，459-470]。这两种形式在结构上相似（CNBr-和葡萄球菌-V8-蛋白酶-裂解肽图谱的标准），并且都对氯化血红素的抑制敏感。但它们与1-氯-2，4-二硝基苯的动力学参数差异很大，且在苯巴比妥的诱导下表现出差异性。这些结果表明，类似的异质性在Ya-亚基，以前描述的Yb-亚基的谷胱甘肽S-转移酶，并表明，显着的基因重复可能发生在这些多功能的细胞内结合蛋白。
CM-cellulose chromatography of rat liver and kidney cytosol at pH6 reveals the presence of a second Ya-subunit dimer of glutathione S-transferase (GST-F) in addition to the recently described GST-YaYa (GST-L; our nomenclature) [Hayes & Clarkson (1982) Biochem. J. 207, 459-470]. The two forms are structurally similar (by the criteria of CNBr- and Staphylococcus-V8-proteinase-cleavage peptide maps), and both are sensitive to inhibition by haemin. However, their kinetic parameters with 1-chloro-2,4-dinitrobenzene are quite distinct, and they show differential inducibility by phenobarbitone. These results suggest a similar heterogeneity in Ya-subunits to that previously described for Yb-subunits of glutathione S-transferase and indicate that significant gene duplication may have occurred in these multifunctional intracellular binding proteins.