l-乳酸蛋白水解产生的细胞色素b2核的性质:酵母细胞色素c氧化还原酶

Françoise Labeyrie , Olga Groudinsky , Yvette Jacquot-Armand , Liliane Naslin
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引用次数: 52

摘要

1.1. 细胞色素b2(酵母l-乳酸:细胞色素c氧化还原酶,EC 1.1.2.3)的胰蛋白酶水解可释放一种细胞色素多肽,该多肽可通过凝胶过滤与其他片段分离。该新产物被称为“noyau cytochromique b2”,其性质已被研究:该分子的分子量约为11000,与一个血红素基团相关;它的光谱性质在可见区与细胞色素b2非常相似。氧化还原电位为- 0.028 V,相对于细胞色素b2 (pH 7.00;30°)。通过电泳检测出几种不同的成分。这些数据已用于乳酸脱氢酶活性分子的结构方面的讨论。
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Propriétés d'un noyau cytochromique b2 résultant d'une protéolyse de la l-lactate: Cytochrome c oxydoréductase de la levure

  • 1.

    1. The tryptic hydrolysis of cytochrome b2 (yeast l-lactate: cytochrome c oxidoreductase, EC 1.1.2.3) liberates a cytochromic polypeptide which can be separated from the other fragments by gel filtration.

  • 2.

    2. The properties of this new product, called “noyau cytochromique b2”, have been investigated: the molecular weight is about 11 000 and this molecule is associated with one heme group; its spectral properties are very similar in the visible region to those of cytochrome b2. The redox potential is −0.028 V to be compared with the value 0.000 V relative to cytochrome b2 (pH 7.00; 30°). Severa, different components have been detected by electrophoresis. These data have been used in a discussion on the structural aspects of the active molecule of lactate dehydrogenase.

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