1999年12月
Enhancement of lipocalin-type prostaglandin D synthase enzyme activity by guanidine hydrochloride
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- ,
- ,
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- 巻
- 266
- 号
- 3
- 開始ページ
- 641
- 終了ページ
- 646
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1006/bbrc.1999.1881
- 出版者・発行元
- ACADEMIC PRESS INC
The characterization of unfolding of mouse recombinant lipocalin-type prostaglandin D synthase (L-PGDS) by guanidine hydrochloride (GdnHCl) was carried out. In the presence of low concentrations of GdnHCl (up to 0.75 M), enhancement of the enzyme activity was observed. However, above a 1 M concentration of GdnHCl, the enzyme activity was reduced in a concentration-dependent manner. The maximum enzyme activity induced by GdnHCl was approximately 1.5-fold compared with the activity under physiological conditions without GdnHCl. The ellipticity in circular dichroism (CD) spectrum of the L-PGDS at 218 nm, reflecting the P-sheet content, was decreased by GdnHCl (up to 0.75 M), and the minimum ellipticity was observed at 0.5 M GdnHCl. The fluorescence quenching of the intrinsic tryptophan of L-PGDS due to the binding of bilirubin in the presence or absence of GdnHCl was measured. The Kd values obtained in the presence and absence of 0.5 M: GdnHCl were 447 and 115 nM, respectively, indicating lower affinity of the L-PGDS for bilirubin with GdnHCl than without it. Further, an NMR study revealed that the reorganization of hydrogen-bond network in the L-PGDS was observed in the presence of 0.5 M GdnHCl. These results, taken together, indicate that the enzyme activity of L-PGDS is enhanced by the conformational change, especially by the change in the secondary structure. (C) 1999 Academic Press.
- リンク情報
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- DOI
- https://doi.org/10.1006/bbrc.1999.1881
- CiNii Articles
- http://ci.nii.ac.jp/naid/80011456923
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/10603301
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000084735400005&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1006/bbrc.1999.1881
- ISSN : 0006-291X
- CiNii Articles ID : 80011456923
- PubMed ID : 10603301
- Web of Science ID : WOS:000084735400005