Suppr超能文献

5-S-半胱氨酰多巴作为酪氨酸酶的底物。

5-S-cysteinyldopa as a substrate for tyrosinase.

作者信息

Hansson C, Rorsman H, Rosengren E

出版信息

Acta Derm Venereol. 1980;60(5):399-402.

PMID:6162310
Abstract

Oxidation of 5-S-cysteinyldopa by mushroom tyrosinase was studied by measuring 5-S-cysteinyldopa consumption with HPLC. 5-S-cysteinyldopa was found to be a substrate for tyrosinase, but our results suggests that a self-catalysed oxidation induced by enzymatically formed 5-S-cysteinyl dopaquinone also takes place. Dopa oxidation by tyrosinase was determined by measuring substrate consumption with HPLC. The oxidation of 5-S-cysteinyldopa was markedly accelerated in the presence of dopa. This could be explained by dopaquinone oxidation of 5-S-cysteinyldopa, which has a lower oxidation potential than dopa.

摘要

通过高效液相色谱法(HPLC)测定5-S-半胱氨酰多巴的消耗,研究了蘑菇酪氨酸酶对5-S-半胱氨酰多巴的氧化作用。发现5-S-半胱氨酰多巴是酪氨酸酶的底物,但我们的结果表明,由酶促形成的5-S-半胱氨酰多巴醌诱导的自催化氧化也会发生。通过HPLC测定底物消耗来确定酪氨酸酶对多巴的氧化作用。在多巴存在下,5-S-半胱氨酰多巴的氧化明显加速。这可以用5-S-半胱氨酰多巴的多巴醌氧化来解释,其氧化电位低于多巴。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验