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首页> 美国卫生研究院文献>The Journal of Clinical Investigation >Membrane-bound cytochrome b5 reductase (methemoglobin reductase) in human erythrocytes. Study in normal and methemoglobinemic subjects.
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Membrane-bound cytochrome b5 reductase (methemoglobin reductase) in human erythrocytes. Study in normal and methemoglobinemic subjects.

机译：人红细胞中的膜结合细胞色素b5还原酶（高铁血红蛋白还原酶）。在正常和高铁血红蛋白病受试者中进行研究。

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摘要

In this study we present evidence that in human erythrocytes NADH-cytochrome b5 reductase (methemoglobin reductase) is not only soluble but also tightly bound to the membrane. The membrane methemoglobin reductase-like activity is unmasked by Triton X-100 treatment, and represents about half of the total activity in the erythrocytes. Like the amphiphilic microsomal-bound cytochrome b5 reductase, the erythrocyte membrane-bound enzyme is solubilized by cathepsin D. Because this treatment is effective on unsealed ghosts but not on resealed (inside-in) ghosts, it is concluded that the enzyme is strongly bound to the inner face of the membrane. The erythrocyte membrane enzyme is antigenically similar to the soluble enzyme. The two forms of enzyme are specified by the same gene, in that both were found defective in six patients with recessive congenital methemoglobinemia. We suggest that the cytochrome b5 reductase of the erythrocyte membrane is the primary gene product. A posttranslational partial proteolysis probably gives rise to the soluble form of the enzyme, which serves as a methemoglobin reductase.
机译：在这项研究中，我们提供的证据表明，在人类红细胞中，NADH-细胞色素b5还原酶（高铁血红蛋白还原酶）不仅可溶，而且与膜紧密结合。膜高铁血红蛋白还原酶样活性没有被Triton X-100处理所掩盖，约占红细胞总活性的一半。像两亲性微粒体结合的细胞色素b5还原酶一样，红细胞膜结合的酶也被组织蛋白酶D溶解。由于这种处理方法对未密封的鬼魂有效，但对重新密封的（内部-内部）鬼魂无效，因此得出结论，该酶被牢固地结合到膜的内表面红细胞膜酶在抗原上类似于可溶性酶。这两种酶的形式由同一基因指定，因为在六名隐性先天性高铁血红蛋白血症患者中发现这两种酶均存在缺陷。我们建议，红细胞膜的细胞色素b5还原酶是主要的基因产物。翻译后部分蛋白水解可能产生该酶的可溶性形式，该酶充当高铁血红蛋白还原酶。

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