Detection of structural change of superoxide dismutase in solution.

نویسندگان

  • Yuji Chiba
  • Yuichi Sutoh
  • Yuzo Nishida
چکیده

We have confirmed that dissociation of the dimeric SOD molecule into a monomeric one can be readily detected in solution by the use of capillary electrophoresis (CE), which is based on the fact that the peak height in the CE profile is highly dependent on the aggregation conditions of the protein molecule. Based on this fact, it has become apparent that the hydrogen peroxide molecule induces the dissociation of the dimeric structure of SOD, and this should give reasonable explanation for the inactivation of SOD by hydrogen peroxide. Our results may give a convenient way for the early detection of the amyotrophic lateral sclerosis in patients, because we can estimate whether the SOD molecule is of a rigid or loosed dimeric structure by the use of this technique. The loosed one has been assumed to exhibit inherent toxicity of the copper center, so-called "gain-of-function" of the mutant SOD.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Study the effect of eight weeks incremental aerobic exercise training with zinc supplementation on Muscular Enzymatic activity of superoxide dismutase and serum leptine in adult male wistar rats

Background & Objective: The purpose of study, was to investigate the effect of 8weeks incremental aerobic training with zinc supplementation on muscular enzymatic activity of superoxide dismutase and serum leptine in wistar rats. Materials & Methods: 32 Wistar rats, randomly divided into 4groups (control, training, training +zinc and zinc). The training protocol consisted of running on treadmil...

متن کامل

Modeling, Mutagenesis and In-silico Structural Stability Assay of the Model of Superoxide Dismutase of Lactococcus Lactis Subsp. Cremoris MG1363

Background:Characterizing the structure and function of superoxide dismutase (SOD), as an antioxidant enzyme providing opportunities for its application in food supplements. Objectives: In this study, the features of the Manganese-SOD of Lactococcus lactis (SDLL), subsp. cremoris MG1363, as probiotic bacteria, were determined on the ...

متن کامل

Human Erythrocyte Superoxide Dismutase Encapsulated in Positively Charged Liposomes

      Superoxide dismutase (SOD) is an important antioxidant that protects many types of cells from the free radical damage. One of the possible ways for the use of SOD is its incorporation in liposomes. The aim of this study was to investigate the effect of cationic phospholipids on the entrapment of human erythrocyte superoxide dismutase (Cu/Zn SOD) in liposomes. Also, in the present study, w...

متن کامل

The Effect of Different Polyamines on Some Physiological Traits as ACC Oxidase and Superoxide Dismutase Enzymes Activity in Chrysanthemum morifolium cv. ‘Bright Golden Ann’

This experiment was conducted to determine the effect of foliar spray with polyamines on postharvest life of chrysanthemum cut flowers in the horticulture laboratory of Islamic Azad University of Rafsanjan in 2015. For this purpose, an experiment was conducted based on a completely randomized design with three replications with spermidine, spermine and putrescine treatments at 1, 2 and 3 mM con...

متن کامل

Comparative modelling of 3D-structure of Geobacter sp. M21 (a metal reducing bacteria) Mn-Fe superoxide dismutase and its binding properties with bisphenol-A, aminotriazole and ethylene-diurea

Superoxide dismutase play important roles in iron-respiratory bacteria such as Geobacteraceae as an antioxidant defense, and probably an effective enzyme of electron transfer network. Regarding the application of iron-respiratory bacteria in environmental biotechnology particularly biodegradation and bioremediation, understanding the mechanism of inhibition/induction of superoxide dismutase by ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Zeitschrift fur Naturforschung. C, Journal of biosciences

دوره 61 3-4  شماره 

صفحات  -

تاریخ انتشار 2006