USE OF CYPRIDINA LUCIFERIN ANALOG FOR ASSESSING THE MONOAMINE OXIDASE-LIKE SUPEROXIDE-GENERATING ACTIVITIES OF TWO PEPTIDE SEQUENCES CORRESPONDING TO THE HELICAL COPPER-BINDING MOTIF IN HUMAN PRION PROTEIN AND ITS MODEL ANALOG
USE OF CYPRIDINA LUCIFERIN ANALOG FOR ASSESSING THE MONOAMINE OXIDASE-LIKE SUPEROXIDE-GENERATING ACTIVITIES OF TWO PEPTIDE SEQUENCES CORRESPONDING TO THE HELICAL COPPER-BINDING MOTIF IN HUMAN PRION PROTEIN AND ITS MODEL ANALOG
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使用荧光素荧光素类似物评估人朊病毒蛋白中与螺旋铜结合基序相对应的两个肽序列的单胺氧化酶样超氧化物生成活性及其模型类似物
DOI:
10.1142/9789812839589_0019
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发表时间:
2008
期刊:
影响因子:
--
通讯作者:
T. Kawano
中科院分区:
文献类型:
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作者:
Ken Yokawa;T. Kagenishi;T. Kawano
In this study, we compared the O2"-generating activity of two peptide sequences corresponding to the PrP helical Cu-binding site namely the model analog sequence often employed in the biochemical studies, 34 and the original sequence found in the native PrP, using Cypridina luciferin analog (CLA) as a chemiluminescent probe for O₂MATERIALS The model sequence for PrP helical Cu-binding region (VNITKQHTVTTTT) proposed by Brown et al. ¹ was used since this sequence was shown to be active as the catalyst for generation of O2 in presence of some aromatic monoamines. 3 Additionally, a peptide corresponding to the natural helical sequence, VNITIKQHTVTTTT, was also prepared (Fig. 1). Two peptides were chemically synthesized and purified on HPLC (purity, 99.20%, 99.10%, respectively) by Sigma Genosis Japan (Ishikari, Hokkaido).