Kinetics studies on triacontanyl palmitate: a urease inhibitor.

The mechanism of inhibition of jack bean and Bacillus pasteurii ureases was investigated by triacontanyl palmitate (1) which is a long-chain fatty ester and has been isolated from Symplocos racemosa Roxb. Lineweaver-Burk, Dixon plots, and their secondary replots showed that 1 is a non-competitive in...

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Publicado en:Natural Product Research Vol. 21; no. 8; pp. 721 - 726
Autores principales: Lodhi, Muhammad Arif, Abbasi, Muhammad Athar, Choudhary*, Muhammad Iqbal, Ahmad, Viqar Uddin
Formato: Journal Article
Publicado: Taylor & Francis Ltd Jul2007
Acceso en línea:Ver este registro en EBSCOhost
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      dt: Jul2007
      vid: 21
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      pub: Taylor & Francis Ltd
      place: Philadelphia, Pennsylvania
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        atl: Kinetics studies on triacontanyl palmitate: a urease inhibitor.
      aug:
        au:
          Lodhi, Muhammad Arif
          Abbasi, Muhammad Athar
          Choudhary*, Muhammad Iqbal
          Ahmad, Viqar Uddin
        affil: Dr Panjwani Center for Molecular Medicine and Drug Research, HEJ Research Institute of Chemistry, International Center for Chemical Sciences, University of Karachi, Karachi-75270, Pakistan
      sug:
      ab: The mechanism of inhibition of jack bean and Bacillus pasteurii ureases was investigated by triacontanyl palmitate (1) which is a long-chain fatty ester and has been isolated from Symplocos racemosa Roxb. Lineweaver-Burk, Dixon plots, and their secondary replots showed that 1 is a non-competitive inhibitor of these enzymes. Ki values were found to be 60.03 ± 1.72 and 88.23 ± 0.31 µM against jack bean and B. pasteurii ureases, respectively.
      pubtype: Academic Journal
      doctype: Journal Article
      ougenre: Article
    language: English
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