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کاربرد نوع شرط:
- جایگاه : پژوهشی
- مجله: Journal of Applied Biotechnology Reports
- نوع مقاله: Journal Article
- کلمات کلیدی: Enzyme-Linked Immunosorbent Assay (ELISA),Glomerular filtration rate (GFR),Creatinine,Cystatin C
- چکیده:
- چکیده انگلیسی: Introduction: Chronic kidney disease is a worldwide health problem and Glomerular filtration rate (GFR) is the most frequently used criteria in the assessment of rental function. Cystatin C as a member of type 2 cystatin superfamily and cysteine-protease inhibitor is found in high concentrations in all biological fluids. This study is aimed to study cystatin C as a potent biomarker for clinical measurement of renal disorders and other diseases.
Materials and Methods: In this study, the human cystatin C construct was analyzed by bioinformatics software. It was cloned and expressed to produce an appropriate antigen for anti-cystatin C (anti-Cys C) obtained from mice Balb/C as a crucial point in the improvement of an enzyme-linked immunosorbent assay (ELISA) method. Serum samples were given from 32 hospitalized patients with renal failure and cardiovascular disease and non-hospitalized patients were tested by ELISA method using anti-Cys C obtained from mice Balb/C.
Results: Our findings indicated 0.36-2.4 mg/L as the best conclusion for antigen cystatin C in patients’ sera and 1/50 dilution for anti-Cys C obtained from mice Balb/C and showed a relationship between patients with high creatinine and high concentration of cystatin C. In case of five cardiovascular disease patients with normal upper limit of Creatinine we obtained cystatin C lower than kidney failure and raising of cystatin C in 6 patients with increased TSH were seen.
Conclusions: Polyclonal anti-Cys C antibodies were obtained through the immunization of Balb/C mice can be employed as an anti-Cys C in ELISA for diagnosis of some renal dysfunction.- انتشار مقاله: 20-08-1396
- نویسندگان: Zahra Abdollah,Samaneh Khodi,Elaheh Gheybi,Jafar Amani,Ali Karami
- مشاهده
- جایگاه : پژوهشی
- مجله: Journal of Applied Biotechnology Reports
- نوع مقاله: Journal Article
- کلمات کلیدی: FPLC,Bacteriorhodopsin,Purple Membrane,Halobacterium,Retinal
- چکیده:
- چکیده انگلیسی: Bacteriorhodopsin operates as a light/proton transfer pump which converts the light energy into a proton gradient. The energy stored in the proton gradient can be used in a variety of ways. The main source of Bacteriorhodopsin are some Halobacterium species such as Halobacterium sodomense and Halobacterium salinarum which grow in harsh and salt-saturated conditions. In order to isolate strains from Aran-Bidgol Lake, two red pigment (IRLS.1) and orange pigment (IRLS.2) strains were isolated. Spectroscopy reviews and the results of SDS-Page of membrane proteins of two isolated strains as well as Iranian native Halobacterium salinarum showed that bacteriorhodopsin protein presents in the collected sample. Spectroscopic studies showed that Halobacterium salinarum produces the maximum amount than IRLS.1 and IRLS.2 produces less and lesser amount of bacteriorhodopsin respectively. The results of biochemical and molecular identification based on the 16srRNA of both mentioned strains indicated their highest similarity with Natrinema sp. XA3-1 and Archaeon RC34, respectively. In this study, the presence of bacteriorhodopsin protein in Iranian native strains was examined for the first time and the local strains were isolated purely from Halobacterium salinarum membrane by gel filtration chromatography that given the widespread use of bacteriorhodopsin protein, it will be so effective.
- انتشار مقاله: 25-06-1395
- نویسندگان: Sahar Shakuri,Ali Mohammad Latifi,Morteza Mirzaei,Samaneh Khodi
- مشاهده
- جایگاه : پژوهشی
- مجله: Journal of Applied Biotechnology Reports
- نوع مقاله: Journal Article
- کلمات کلیدی: Biodegradation,Organophosphates Toxicity,Hydrolysis Enzyme
- چکیده:
- چکیده انگلیسی: Daily, organophosphorus compounds (OPs) in human life, has found wide applications. Although OPs have biodegradability potential, they induce clinical problems in humans and other organism. Different methods are used to detoxify these compounds. In the meantime, biodegradation is preferred as a compatible way to the environment since it produces less toxic compounds. Enzymes capable to degrade the OPs are of the most important items in the biodegradation. Genetic manipulation involved in the production of these enzymes has been employed in bacteria, and finally, is used for the mass production of recombinant microorganisms. In this paper, the role of organophosphates on human life and the ways to destroy toxic organophosphates are studied.
- انتشار مقاله: 25-10-1393
- نویسندگان: Safar Ali Ahmadizad Firozjaei,Ali Mohammad Latifi,Samaneh Khodi,Shamsozzoha Abolmaali,Ali Choopani
- مشاهده
- جایگاه : پژوهشی
- مجله: Journal of Applied Biotechnology Reports
- نوع مقاله: Journal Article
- کلمات کلیدی: Recombinant vaccine,Polyclonal antibody,Diphtheria,diphtheria toxin,Mutated DTxA Chain
- چکیده:
- چکیده انگلیسی: Diphtheria is a fatal disease caused by exotoxin of Corynebacterium diphtheria. This toxin consists of two chains, catalytic chain (A) and binding (B) chain. By binding chain (B), the toxin binds to its receptor on numerous body cells such as myocardial, kidney and peripheral nerve cells. After entering, catalytic chain (A) inhibits protein synthesis and finally can cause cell death. At this time, the toxoid form of diphtheria toxin is used as vaccine. The aim of this study was the immunological analysis of the mutated synthetic catalytic subunit of diphtheria toxin in laboratory animals as a vaccine candidate, in addition to polyclonal antibody production and purification against diphtheria toxin. For this purpose the Dtx recombinant protein (with two mutant: A158G and G52E) was expressed using pET28a/DtxA plasmid in E. coli Bl21DE3 host. Then, recombinant protein, as a candidate vaccine, was extracted and purified. After evaluating and confirming the protein by SDS-PAGE and western blotting, immunization carried out in laboratory animals. Finally, followed by antibody titration by ELISA, antibody purification performed as well.The mutated recombinant protein prepared from an optimized expression was extracted and purified. Then, this protein was confirmed by SDS-PAGE and western blotting. ELISA results showed a satisfactory immunization of animals by this protein. Polyclonal antibody production and purification against diphtheria toxin was performed by G protein column and confirmed by ELISA. ELISA results showed a high titer of polyclonal antibody against diphtheria toxin in animal's serum after immunization by recombinant DTx protein.
- انتشار مقاله: 08-01-1397
- نویسندگان: Mohammad Ali Arefpour Torabi,Gholam Reza Olad,Shahram Nazarian,Jafar Salimian,Samaneh Khodi,Mohamad Javad Bagheripour
- مشاهده