MISC

1999年12月

Enhancement of lipocalin-type prostaglandin D synthase enzyme activity by guanidine hydrochloride

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  • T Inui
  • ,
  • T Ohkubo
  • ,
  • Y Urade
  • ,
  • O Hayaishi

266
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
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
  • DOI : 10.1006/bbrc.1999.1881
  • ISSN : 0006-291X
  • CiNii Articles ID : 80011456923
  • PubMed ID : 10603301
  • Web of Science ID : WOS:000084735400005

エクスポート
BibTeX RIS