Purification of Copper-Zinc Superoxide Dismutase from Human Erythrocytes and Partial Characterization

Karadag, Hasan; Bilgin, Ramazan

doi:10.2478/v10133-010-0021-7

Cited by 8 publications

(3 citation statements)

References 12 publications

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“…Al-Gazaly found that SOD from human RBCs (control) was purified using ionexchange chromatography (IEC) 10671.4 fold with a yield of 73.3% and its specific activity was 2955.98 U/mg of protein, while SOD from chronic children diarrhea was purified 16256.67 fold with a yield of 83.469 and its specific activity was 6502.67 U/ml of protein [21]. While Karadag and Bilgin who purified SOD from human RBCs, reported 20.2 fold with a yield of 55.1% and specific activity was 155.41 U/mg of protein after using (IEC) method [4].…”

Section: Resultsmentioning

confidence: 99%

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A Comparative Study of Superoxide Dismutase Purification from Red Blood Cells of Near Residents to Cellular Phone Base-Stations Antennas

2019

University of Thi-Qar Journal

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Superoxide dismutase (SOD) is the first line of defense against reactive oxygen species (ROS) such as the superoxide radical which is a toxic to living cells as it oxidizes and degrades biological molecules such as lipids and proteins. In the present study, SOD was purified from red blood cells (RBCs) of individuals who were living nearby the cellular phone base-station and others who living far from these stations. Over the last 10 years, there has been a wide spread in the use of cellular phones in Iraq, the communication system which can require hundreds of antennas in close proximity to the population with exposure to the radiation. The emitted radiation from these antennas may affect the biological systems. The aim of this work was to comprise the purification of SOD from RBCs of two individual groups. The first group (G1) was included individuals who reside near from mobile phone base-station, and the second group (G2) was included the individuals who inhabit far from these stations. We applied a simple and rapid procedure for the purification by ion exchange chromatography on diethylaminoethyl (DEAE)-Sepharose column. SOD was purified with a fold of purification of 20.6, yield of 47.5 %, SOD specific activity was 2948 (U/mg) for G1, while for the G2 the fold of purification was equal to 15.4 with a yield of 20.6% and 2143 (U/mg) as a specific activity of SOD. This procedure appears, therefore, to be a convenient and easily method for isolating this enzyme.

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Section: Resultsmentioning

confidence: 99%

“…Web Site: https://jutq.utq.edu.iq/index.php/main Email: journal@jutq.utq.edu.iq 2 concerning SOD was carried out by Mann and Keilin in 1938 [4]. SODs are classified into four groups depending on their metal cofactors: MnSOD, Cu-ZnSOD, FeSOD and NiSOD [5].…”

Section: University Of Thi-qar Journal Vol10 No1 Mar 2015mentioning

confidence: 99%

A Comparative Study of Superoxide Dismutase Purification from Red Blood Cells of Near Residents to Cellular Phone Base-Stations Antennas

2019

University of Thi-Qar Journal

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“…Although H 2 O 2 is not itself a free radical it can be toxic at high concentrations, so it is broken down into water by catalase in peroxisomes and glutathione peroxidase in the cytosol and mitochondria [ 4 ]. SOD has been purified from diverse sources such as: fungi [ 6 ]; bacteria [ 7 ]; yeast [ 8 ]; plants [ 9 ] and animals [ 10 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning, Characterization and Predicted Structure of a Putative Copper-Zinc SOD from the Camel, Camelus dromedarius

Ataya

Fouad

Al-Olayan

et al. 2012

IJMS

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Superoxide dismutase (SOD) is the first line of defense against oxidative stress induced by endogenous and/or exogenous factors and thus helps in maintaining the cellular integrity. Its activity is related to many diseases; so, it is of importance to study the structure and expression of SOD gene in an animal naturally exposed most of its life to the direct sunlight as a cause of oxidative stress. Arabian camel (one humped camel, Camelus dromedarius) is adapted to the widely varying desert climatic conditions that extremely changes during daily life in the Arabian Gulf. Studying the cSOD1 in C. dromedarius could help understand the impact of exposure to direct sunlight and desert life on the health status of such mammal. The full coding region of a putative CuZnSOD gene of C. dromedarius (cSOD1) was amplified by reverse transcription PCR and cloned for the first time (gene bank accession number for nucleotides and amino acids are JF758876 and AEF32527, respectively). The cDNA sequencing revealed an open reading frame of 459 nucleotides encoding a protein of 153 amino acids which is equal to the coding region of SOD1 gene and protein from many organisms. The calculated molecular weight and isoelectric point of cSOD1 was 15.7 kDa and 6.2, respectively. The level of expression of cSOD1 in different camel tissues (liver, kidney, spleen, lung and testis) was examined using Real Time-PCR. The highest level of cSOD1 transcript was found in the camel liver (represented as 100%) followed by testis (45%), kidney (13%), lung (11%) and spleen (10%), using 18S ribosomal subunit as endogenous control. The deduced amino acid sequence exhibited high similarity with Cebus apella (90%), Sus scrofa (88%), Cavia porcellus (88%), Mus musculus (88%), Macaca mulatta (87%), Pan troglodytes (87%), Homo sapiens (87%), Canis familiaris (86%), Bos taurus (86%), Pongo abelii (85%) and Equus caballus (82%). Phylogenetic analysis revealed that cSOD1 is grouped together with S. scrofa. The predicted 3D structure of cSOD1 showed high similarity with the human and bovine CuZnSOD homologues. The Root-mean-square deviation (rmsd) between cSOD1/hSOD1 and cSOD1/bSOD1 superimposed structure pairs were 0.557 and 0.425 A. The Q-score of cSOD1-hSOD1 and cSOD1-bSOD1 were 0.948 and 0.961, respectively.

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Enhancing the Purification and Stability of Superoxide Dismutase by Fusion with Thermoresponsive Self‐Assembly of Elastin Like Polypeptide

Wang,

Xia

et al. 2024

ChemistrySelect

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Elastin‐like polypeptide (ELP) is a thermo‐sensitive biosynthetic polymer composed of a Val‐Pro‐Gly‐Xaa‐Gly repeating unit possessing a sharp reversible phase transition property at specific temperatures. Here, ELP was fused to human superoxide dismutase 1 (hSOD1) modified with His tag to produce recombinant hSOD1‐Linker‐ELP‐His (hSODLEH) which was expressed in E. coli and purified via inverse thermal cycling (ITC) and Ni‐NTA resin. The results showed that ELP tag did not affect the soluble expression of SOD1. The purification by ITC was superior to Ni‐NTA resin due to its convenient purification process, improved recovery rate and purification fold, thus indicating industrial suitability for large scale protein purification in a cost‐ and time‐efficient manner. Moreover, one round of ITC was sufficient for the recovery of highly purified recombinant SOD. The results further showed that ELP improved the stability of the SOD, and did not affect its secondary structure nor its ability to bind divalent metal ions. Overall, ELP‐protein fusion system could be a promising tool for large scale enzyme purification.

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Purification of Copper-Zinc Superoxide Dismutase from Human Erythrocytes and Partial Characterization

Cited by 8 publications

References 12 publications

A Comparative Study of Superoxide Dismutase Purification from Red Blood Cells of Near Residents to Cellular Phone Base-Stations Antennas

A Comparative Study of Superoxide Dismutase Purification from Red Blood Cells of Near Residents to Cellular Phone Base-Stations Antennas

Molecular Cloning, Characterization and Predicted Structure of a Putative Copper-Zinc SOD from the Camel, Camelus dromedarius

Enhancing the Purification and Stability of Superoxide Dismutase by Fusion with Thermoresponsive Self‐Assembly of Elastin Like Polypeptide

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