Increase in Molecular Rigidity of the Protein Conformation of Brain Na〔+〕-K〔+〕-ATPase by Modification with 4-Hydroxy-2-nonenal
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- Miyake Hiromi
- Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University
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- Kadoya Akinori
- Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University
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- Ohyashiki Takao
- Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University
書誌事項
- タイトル別名
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- Increase in Molecular Rigidity of the Protein Conformation of Brain Na+-K+-ATPase by Modification with 4-Hydroxy-2-nonenal
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説明
The effect of lipid peroxidation product 4-hydroxy-2-nonenal (HNE) on the protein conformation of porcine cerebral cortex Na+–K+-ATPase was examined in term of the intrinsic tryptophanyl fluorescence measurement. Treatment of ATPase with HNE resulted in a decrease in the fluorescence intensity and an increase in the fluorescence anisotropy in a concentration-dependent manner. The difference in the fluorescence intensity and fluorescence anisotropy observed between the control and HNE-modified ATPase completely disappeared after treatment of the protein with guanidine hydrochloride (1 M). These results suggest that HNE-modification of the Na+–K+-ATPase induces alterations in the conformation of the enzyme molecule. This interpretation was further supported by a decrease in fluorescence quenching efficiency with acrylamide and sulfhydryl (SH) content. The decrease in quenching efficiency suggests that the proximity of the quencher molecule to the fluorophores located in the enzyme is suppressed. Modification of the enzyme with N-ethylmaleimide (NEM) also resulted in a decrease in quenching efficiency with the loss of SH groups. Furthermore, a good relationship between the SH content and these fluorescence parameters (fluorescence anisotropy and quenching efficiency) were observed. On the other hand, treatment of the Na+–K+-ATPase with other aldehydes such as malondialdehyde (MDA), 1-hexanal and nonanal did not affect either the quenching efficiency or SH content. Based on these results, the possibility of alterations in the physical properties of the Na+–K+-ATPase associated with modification by HNE has been discussed.
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 26 (12), 1652-1656, 2003
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390001204626114048
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- NII論文ID
- 110003608367
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- NII書誌ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 6766631
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- PubMed
- 14646165
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- PubMed
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- 使用不可