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细胞色素C来源的血红素十一肽介导的晶状体晶状体蛋白快速H2O2介导的非光动力学交联:对人类白内障发生的潜在影响。

The rapid H2O2-mediated nonphotodynamic crosslinking of lens crystallins generated by the heme-undecapeptide from cytochrome C: potential implications for cataractogenesis in man.

作者信息

Bodaness R S, Zigler J S

出版信息

Biochem Biophys Res Commun. 1983 Jun 15;113(2):592-7. doi: 10.1016/0006-291x(83)91767-9.

DOI:10.1016/0006-291x(83)91767-9
PMID:6307294
Abstract

Human cataract lens crystallins are crosslinked and demonstrate a non-tryptophan blue fluorescence. We report here that exposure of lens crystallin to H2O2 within the concentration range reported for human aqueous humor, produces crosslinking of crystallin polypeptides within 10 minutes in the presence of the heme-undecapeptide from cytochrome c. Concomitantly, a blue fluorescence develops. These findings suggest the possibility that under some conditions hydrogen peroxide activation may play a role in cataractogenesis in vivo.

摘要

人类白内障晶状体中的晶状体蛋白发生交联,并呈现出非色氨酸蓝色荧光。我们在此报告,在人房水报道的浓度范围内,将晶状体蛋白暴露于过氧化氢中,在细胞色素c的血红素十一肽存在的情况下,10分钟内晶状体蛋白多肽就会发生交联。同时,会产生蓝色荧光。这些发现表明,在某些条件下,过氧化氢激活可能在体内白内障形成过程中起作用。

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The rapid H2O2-mediated nonphotodynamic crosslinking of lens crystallins generated by the heme-undecapeptide from cytochrome C: potential implications for cataractogenesis in man.细胞色素C来源的血红素十一肽介导的晶状体晶状体蛋白快速H2O2介导的非光动力学交联:对人类白内障发生的潜在影响。
Biochem Biophys Res Commun. 1983 Jun 15;113(2):592-7. doi: 10.1016/0006-291x(83)91767-9.
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An analysis of the H2O2-mediated crosslinking of lens crystallins catalyzed by the heme-undecapeptide from cytochrome c.细胞色素c中血红素十一肽催化的过氧化氢介导的晶状体晶状体蛋白交联分析。
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Cross-linking of lens crystallins in a photodynamic system: a process mediated by singlet oxygen.光动力系统中晶状体晶状体蛋白的交联:单线态氧介导的过程。
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The H2O2-mediated oxidation of NADPH to NADP+ catalyzed by the heme-undecapeptide from cytochrome C.由细胞色素C的血红素十一肽催化的H2O2介导的NADPH氧化为NADP+的反应。
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Changes in lens proteins induced at the early stage of cataractogenesis in cac (Nakano) mice.在cac(中野)小鼠白内障发生早期诱导的晶状体蛋白变化。
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Formation of hydrogen peroxide by lens proteins: protein-derived hydrogen peroxide as a potential mechanism of oxidative insult to the lens.
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