Studies on cytochrome c oxidase, IX. The primary structure of polypeptide VIa.
Studies on cytochrome c oxidase, IX. The primary structure of polypeptide VIa.
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细胞色素c氧化酶的研究，IX。
DOI：
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发表时间：
1982
期刊：
影响因子：
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通讯作者：
G. Buse
中科院分区：
文献类型：
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作者：
R. Biewald;G. Buse
描述了来自牛心的细胞色素c氧化酶的细胞质多肽VIa的完整氨基酸序列。通过用金黄色葡萄球菌蛋白酶、来自小鼠颌下腺的蛋白酶、2-碘酰基苯甲酸和溴化氰切割获得的重叠谷氨酸、精氨酸、色氨酸和蛋氨酸片段的分离和测序，阐明了呼吸链复合体 IV 的该组分的一级结构。多肽VIa的链长为98个氨基酸，所得分子量为10670Da。亲水性蛋白质不包含疏水性膜穿透序列结构域。其在呼吸复合体 IV 中的功能尚不清楚。
The complete amino acid sequence of the cytoplasmic polypeptide VIa of cytochrome c oxidase from beef heart is described. The primary structure of this component of complex IV of the respiratory chain is elucidated by isolation and sequencing of overlapping glutamic acid, arginine, tryptophan and methionine fragments obtained by cleavage with Staphylococcus aureus protease, protease from submaxillaris glands of mice, 2-iodosylbenzoic acid and cyanogen bromide. The chain length of polypeptide VIa is 98 amino acids, the resulting molecular mass of 10670 Da. The hydrophilic protein does not contain a hydrophobic membrane penetrating sequence domain. Its function in the respiratory complex IV is unknown.