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De Marqui, A.B.T., Vidotto, A., Polachini, G.M., Bellato, C.D.M., Cabral, H., Leopoldino, A.M., et al. (2006) Solubilization of Proteins from Human Lymph Node Tissue and Two-Dimensional Gel Storage. Journal of Biochemistry and Molecular Biology, 39, 216-222.
https://doi.org/10.5483/BMBRep.2006.39.2.216

has been cited by the following article:

• TITLE: Analysis of Two-Dimensional Gel Electrophoresis Map of Methicillin-Resistant Staphylococcus aureus Treated with Acetone Extract from Canarium odontophyllum Miq. Leaves

  AUTHORS: Nur Amira Mohd Shamsuddin, Dayang Fredalina Basri, Noraziah M. Zin, Ahmad Raha Raus, Nur Faizah Abu Bakar

  KEYWORDS: Canarium odontophyllum, MRSA, 2-DE, IEF, SDS-PAGE Protein Expression Profile

  JOURNAL NAME: American Journal of Plant Sciences, Vol.12 No.1, January 22, 2021

  ABSTRACT: Methicillin-resistant Staphylococcus aureus (MRSA) infection is a global health concern that has caused severe health threats over the past decade. Leaves extract of C. odontophyllum has been proven previously as an anti MRSA agent. Proteomics provide a technique that used to analyze the differential of protein expression profile between untreated and treated MRSA with subinhibitory concentrations of acetone extract from C. odontophyllum leaves. This study aims to determine the optimum parameter for analysis of protein expression profile using two-dimension gels electrophoresis (2-DE) for MRSA protein after treatment with acetone extract from C. odontophyllum leaves. Comparison of the Protein Expression Profile (PEP) between the untreated and treated MRSA was analyzed using PDQuest software. The optimum condition for MRSA protein treated with acetone extract from C. odontophyllum leaves to produce the best resolution with greater spot distribution was as follows: 100 μg volume of MRSA protein that loaded after passive rehydration then was run until reaching 25 kVrhs during IEF using 17 cm IPG strip within ranges of pH 4 - 7. Analysis of protein expression from the 2-DE gel map shows that 9 protein spots up-regulated and 41 protein spots were down-regulated with more than 2-fold differences (p C. odontophyllum leave may provide an insight into the antimicrobial mechanism, which could lead to the identification of target protein for future novel therapeutic development against MRSA infections.