Characteristics of the fluorescence spectra of apoenzyme and flavin portions of D-amino acid oxidase

Felicia Ying Hsiueh Wu*, Shiao Chun Tu, Cheng-Wen Wu Lee, Donald B. McCormick

*此作品的通信作者

研究成果: Article同行評審

18 引文 斯高帕斯(Scopus)

摘要

The tryptophan fluorescence maxima for semiholo- and holoenzymes of D-amino acid oxidase are blue-shifted from that of the apoenzyme by 10 and 20 nm, respectively. These findings indicate that tryptophan residues of semiholo and holo forms are in a more nonpolar environment and less accessible to water than those in the apoenzyme. Overall, results suggest that some tryptophan residues may be near or at the flavin active site in D-amino acid oxidase.

原文English
頁(從 - 到)381-385
頁數5
期刊Biochemical and Biophysical Research Communications
41
發行號2
DOIs
出版狀態Published - 23 10月 1970

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