Characteristics of the inhibition of hemoglobin synthesis in rabbit reticulocytes by threo-α-amino-β-chlorobutyric acid

M. Rabinovitz, J.M. Fisher
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引用次数: 81

Abstract

  • 1.

    1. Addition of the valine antagonist, α-amino-β-chlorobutyric acid, to rabbit reticulocytes produces a rapid inhibition of hemoglobin synthesis with a subsequent increase in labelling of protein of the ribosomal fraction.

  • 2.

    2. At appropriate antagonist: valine ratios, the incorporation of valine itself occurs at the ribosomal level, but is inhibited in hemoglobin. This indicates that the block in hemoglobin synthesis is caused by substitution of the analogue for valine at specific valine sites, and it is suggested that the loci of these substitutions may be the Val-Val residues on the precursor protein of the β-chain.

  • 3.

    3. The antagonist also inhibits [14C]isoleucine incorporation into hemoglobin, but unlike other amino acids, isoleucine does not accumulate in protein of the ribosomal fraction. This observation is discussed in relation to the characteristics of isoleucine incorporation into reticulocyte proteins and the location of residues of this amino acid near the NH2-terminal end of the α-chain of rabbit hemoglobin.

  • 4.

    4. Synthesis of both the α- and β-chains of hemoglobin is blocked by the antagonist and there is no evidence for the preferential synthesis and release of either chain.

  • 5.

    5. Abortive protein formed in the presence of the antagonist is rapidly degraded into trichloroaceeric acid-soluble products.

三-α-氨基-β-氯丁酸抑制兔网织红细胞血红蛋白合成的特性
1.1. 在兔网织红细胞中加入缬氨酸拮抗剂α-氨基-β-氯丁酸,可快速抑制血红蛋白合成,随后增加核糖体部分蛋白的标记。在合适的拮抗剂缬氨酸比例下,缬氨酸本身的结合发生在核糖体水平,但在血红蛋白中被抑制。这表明血红蛋白合成中的阻滞是由缬氨酸类似物在特定缬氨酸位点的取代引起的,并且这些取代的位点可能是β-链前体蛋白上的Val-Val残基。拮抗剂也抑制[14C]异亮氨酸并入血红蛋白,但与其他氨基酸不同,异亮氨酸不会积聚在核糖体部分的蛋白质中。这一观察结果与异亮氨酸并入网织红细胞蛋白的特性以及该氨基酸残基位于兔血红蛋白α-链的nh2末端有关。血红蛋白α-链和β-链的合成均被拮抗剂阻断,没有证据表明其中任何一条链优先合成和释放。在拮抗剂存在下形成的流产蛋白迅速降解为三氯乙酸溶性产物。
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