哺乳动物组织提取物（“血红素α-亚甲酰加氧酶”）的吡啶血色素裂解活性的非酶性质
Non-enzymic nature of the pyridine haemochrome-cleaving activity of mammalian tissue extracts ('haem alpha-methenyl oxygenase').
作者信息
Colleran E, Carra P O
出版信息
Biochem J. 1970 Oct;119(5):905-11. doi: 10.1042/bj1190905.
Abstract
- The pyridine haemochrome-cleaving activity of extracts from mammalian liver and other tissues is shown conclusively to be entirely non-enzymic in nature and attributable to coupled oxidation with ascorbate. 2. Reduced glutathione probably contributes to the activity indirectly by continuously regenerating the ascorbate to the reduced form. 3. The cleavage shows no specificity for the alpha-methine bridge of pyridine haemochrome. 4. Results are presented suggesting some probable reasons for the erroneous characterization of the activity as an alpha-methine-specific haem-cleaving enzyme (;haem alpha-methenyl oxygenase') by Nakajima and co-workers (e.g. Nakajima, Takemura, Nakajima & Yamaoka, 1963; Nakajima & Gray, 1967).
摘要
- 哺乳动物肝脏及其他组织提取物的吡啶血色素裂解活性已被确凿证明本质上完全是非酶促的，且归因于与抗坏血酸的偶联氧化作用。2. 还原型谷胱甘肽可能通过持续将抗坏血酸再生为还原形式而间接促进该活性。3. 该裂解对吡啶血色素的α-次甲基桥没有特异性。4. 本文给出的结果表明了中岛及其同事（如中岛、竹村、中岛和山冈，1963年；中岛和格雷，1967年）将该活性错误地鉴定为α-次甲基特异性血红素裂解酶（“血红素α-亚甲基加氧酶”）的一些可能原因。
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SOME OBSERVATIONS ON THE BREAKDOWN OF HAEMOGLOBIN.
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