Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis
Manoochehr Messripour,
Soheila Moein
Issue:
Volume 2, Issue 2, December 2018
Pages:
22-26
Received:
19 September 2018
Accepted:
29 September 2018
Published:
30 October 2018
DOI:
10.11648/j.ajcbe.20180202.11
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Abstract: Myasthenia gravis (MG) is an antibody-mediated autoimmune neuromuscular disease, leading to skeletal muscle weakness. The autoantibodies are against acetylcholine receptor (AChR) of the muscle membrane localized at the neuromuscular junction. The early diagnosis of MG is a key factorfor the advanced medical practice, but, it still remains challenging. The objective of this pilot study was to examine the pattern of serum protein electrophoresis in the animal experimental model of MG. Acetylcholine receptor (AChR) was purified from rat (mail Wistar) leg muscle by affinity chromatography. Four rabbits were immunized on day 1, week 4 and week 8 with purified rat leg muscle AChR and assayed for serum anti-AChR antibody titer on blood samples taken on week 2, week 5 and week 9. Control rabbits received an emulsion of phosphate bufferded saline in the adjuant. The serum anti-AChR anybodies were tittered using quenching fluoroimmunoassay. Electrophoresis separation of the serum proteins was performed on a cellulose acetate membrane. Results showed that Immunizations of rabbits induced muscle weakness in the animals together with elevation of serum anti-AChR antibody. During the course of immunizations, percentage of beta-globulin fraction increased gradually from 15.8% to 41.2% whereas, albumin decreased from 68.3% to 43.8%. As determined by cellulose acetate electrophoresis. These results represent proof-of principle data for diagnosis of the acetylcholine receptor-MG subtypes and severity.
Abstract: Myasthenia gravis (MG) is an antibody-mediated autoimmune neuromuscular disease, leading to skeletal muscle weakness. The autoantibodies are against acetylcholine receptor (AChR) of the muscle membrane localized at the neuromuscular junction. The early diagnosis of MG is a key factorfor the advanced medical practice, but, it still remains challengi...
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The Role of Binding Pocket Amino Acid Residues in Substrate Specificity Towards Xanthine Oxidase Enzyme
Issue:
Volume 2, Issue 2, December 2018
Pages:
27-49
Received:
26 October 2018
Accepted:
3 December 2018
Published:
3 January 2019
DOI:
10.11648/j.ajcbe.20180202.12
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Abstract: Xanthine oxidase is one of the most useful molybdenum containing enzymes, which catalyzes a wide range of purine derivative heterocyclic substrates. In order for the interaction between the reactants to take place, the substrates are expected to enter the binding pocket and attain a proper orientation with the help of binding pocket amino acid residues. Therefore, the study is mainly focused to understand the role of binding pocket amino acid residues in providing the substrates proper orientation for the nucleophilic reaction to take place. The binding pocket amino acids residues in particular, Glu802 and Arg880 were proposed to create a hydrogen bonding microenvironment and modulate the near attack conformation (NAC) in the presence of substrates. In order to probe the behavior of the substrates, inside the binding pocket, the electronic structure calculations were performed. Moreover, the activation of the active site was proposed to take place after the acidic proton is abstracted from the HOeq by [bmXOR]-Glu1261. The Oxyanion of the active site is responsible for the nucleophilic attack on the deficient carbon center of the given substrates. In general, the purpose of the study is to relate the roles of amino acid residues in the reactivities of enzyme catalyzed reactions and to determine the most favorable path way during the activation of the active site by Glu1261.
Abstract: Xanthine oxidase is one of the most useful molybdenum containing enzymes, which catalyzes a wide range of purine derivative heterocyclic substrates. In order for the interaction between the reactants to take place, the substrates are expected to enter the binding pocket and attain a proper orientation with the help of binding pocket amino acid resi...
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Bioactive Constituents of Essential Oil from Khaya senegalensis (Desr.) Bark Extracts
Blessing Ikoojo Omotoyinbo,
Ayoola Ebenezer Afe,
Olawale Solomon Kolapo,
Oluseyi Valerie Alagbe
Issue:
Volume 2, Issue 2, December 2018
Pages:
50-54
Received:
15 November 2018
Accepted:
13 December 2018
Published:
22 January 2019
DOI:
10.11648/j.ajcbe.20180202.13
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Abstract: The use of plants in traditional medicines has been a common practice in the medical care of many human cultures and dates back to several thousands of years and pre-dates the introduction of antibiotics and other related drugs due to their great source of phytochemicals which are exploited in all medical systems. These study was aimed at characterizing using Gas Chromatography-Mass Spectrometry (GC/MS) technique, the chemical constituents of the essential oil extracted from the bark of Khaya senegalensis Desr. using methanol-chloroform. Eight compounds were identified which include: Sulfurous acid, decylpentyl ester (0.51%), n-Hexadecanoic acid (12.08%), 1-Pentadecanol (1.84%), 13,16-Octadecadienoic acid, methyl ester (1.71%), Oleic acid (39.16%), Octadecanoic acid (21.9%), Dodecanoyl chloride (3.93%) and cis-11-hexadecenal (18.88%). The presence of these compounds in the the bark of Khaya senegalensis might amongst many other bioactive constituents are responsible for the medicinal properties these plant part exhibits and is been used for in herbal medicines.
Abstract: The use of plants in traditional medicines has been a common practice in the medical care of many human cultures and dates back to several thousands of years and pre-dates the introduction of antibiotics and other related drugs due to their great source of phytochemicals which are exploited in all medical systems. These study was aimed at character...
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