تفکیک حرارتی دمینهای آنزیم آمین اکسیداز جوانه عدس با کالریمتری روبشی افتراقی

موسوی موحدی, علی اکبر and امانی, مجتبی and موسوی نژاد, سیده زهرا and هاشم نیا, صدیقه and احمد, فیضان and فلوریس, جیووانی and مورا, آنا and رضایی طاویرانی, مصطفی and حکیم الهی, غلامحسین and صبوری, علی اکبر and یوسفی, رضا (1386) تفکیک حرارتی دمینهای آنزیم آمین اکسیداز جوانه عدس با کالریمتری روبشی افتراقی. Bioscience, Biotechnology and Biochemistry ــ 71 (7). pp. 1644-1649. شاپا 0916-8451

Text - Published Version

Official URL: http://www.scopus.com/inward/record.url?eid=2-s2.0...


Thermal dissection of lentil seedling amine oxidase domains by differential scanning calorimetry

English Abstract

The relationships between the structural and energetic domains of lentil seedling amine oxidase (LSAO) were investigated using modifiers that target the active site and the carbohydrate moiety of the enzyme. An irreversible inhibitor, aminoguanidine, specifically modified the active site of the lentil enzyme, whereas sodium metaperiodate cleaves carbohydrate moieties covalently bound to the native enzyme. Differential scanning calorimetry (DSC) measurements were made on the modi-fied LSAOs. Deconvolution of the reversible thermal DSC profiles of the modified enzyme gave three subpeaks (energetic domains), each of which was assigned to one of the three structural domains of the native protein. Our results led us to conclude that deglycosylation of LSAO has no effect on thermal stability, whereas binding of the inhibitor imparts more stability to the enzyme.

Item Type:Article
زبان سند : انگلیسی
نویسنده مسئول :علی اکبر موسوی موحدی
Additional Information:cited By (since 1996) 0 ONLINE ISSN:1347-6947
کلیدواژه ها (انگلیسی):Amines; Carbohydrates; Deconvolution; Differential scanning calorimetry; Glycosylation; Thermodynamic stability, Energetic domains; Heat denaturation; Lentil seedling amine oxidases; Thermal dissection, Enzyme inhibition, amine oxidase (copper containing), article; chemistry; differential scanning calorimetry; enzymology; lentil; protein denaturation; protein tertiary structure; seedling, Amine Oxidase (Copper-Containing); Calorimetry, Differential Scanning; Lens Plant; Protein Denaturation; Protein Structure, Tertiary; Seedling, Lens culinaris
Subjects:QU Biochemistry
Divisions:Faculty of Medicine > Department of Basic Sciences > Department of Biophysics
ID Code:1066
Deposited By: MS Soghra Golmaghani
Deposited On:13 Dec 1388 06:56
Last Modified:20 Jan 1393 13:05

Repository Staff Only: item control page

Document Downloads

More statistics for this item...