مطالعه مقایسه ای قفلهای کنفورماسیونی، تفکیک، غیر فعال شدن و پایداری آنزیمهای آمین اکسیداز شیره افوربیا و جوانه عدس

امانی, مجتبی and موسوی موحدی, علی اکبر and فلوریس, جیووانی and لونگو, س and مورا, آنا and موسوی نژاد, سیده زهرا and صبوری, علی اکبر and احمد, فیضان (1383) مطالعه مقایسه ای قفلهای کنفورماسیونی، تفکیک، غیر فعال شدن و پایداری آنزیمهای آمین اکسیداز شیره افوربیا و جوانه عدس. The Protein Journal ــ 24 (3). pp. 183-191. شاپا 1572-3887

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Comparative study of the conformational lock, dissociative thermal inactivation and stability of Euphorbia latex and lentil seedling amine oxidases

English Abstract

The thermal stability of copper/quinone containing amine oxidases from Euphorbia characias latex (ELAO) and lentil seedlings (LSAO) was measured in 100 mM potassium phosphate buffer (pH 7.0) following changes in absorbance at 292 nm. ELAO was shown to be about 10°C more stable than LSAO. The dissociative thermal inactivation of ELAO was studied using putrescine as substrate at different temperatures in the range 47-70°C, and a "conformational lock" was developed using the theory pertaining to oligomeric enzyme. Moreover ELAO was shown to be more stable towards denaturants than LSAO, as confirmed by dodecyl trimethylammonium bromide denaturation curves. A comparison of the numbers of contact sites in inter-subunits of ELAO relative to LSAO led us to conclude that the higher stability of ELAO to temperature and towards denaturants was due to the presence of larger number of contact sites in the conformational lock of the enzyme. This study also gives a putative common mechanism for thermal inactivation of amine oxidases and explains the importance of C-terminal conserved amino acids residues in this class of enzymes. © 2005 Springer Science+Business Media, Inc.

Item Type:Article
زبان سند : انگلیسی
نویسنده اول :مجتبی امانی
نویسنده مسئول :علی اکبر موسوی موحدی
Additional Information:cited By (since 1996) 5
کلیدواژه ها (انگلیسی):amine oxidase (flavin containing); amino acid; buffer; copper; dodecyltrimethylammonium bromide; potassium dihydrogen phosphate; quinone derivative, article; carboxy terminal sequence; comparative study; enzyme inactivation; enzyme stability; Euphorbia; lentil; nucleotide sequence; temperature; thermostability, Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Enzyme Stability; Euphorbia; Heat; Latex; Lens Plant; Models, Molecular; Molecular Sequence Data; Plant Proteins; Protein Conformation; Protein Denaturation; Putrescine; Seedling; Sequence Alignment, Euphorbia; Euphorbia characias; Lens culinaris
Subjects:QU Biochemistry
Divisions:Faculty of Medicine > Department of Basic Sciences > Department of Biophysics
ID Code:1070
Deposited By: MS Soghra Golmaghani
Deposited On:13 Dec 1388 07:39
Last Modified:20 Jan 1393 13:11

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