Displaying all 2 publications

Abstract:
Sort:
  1. Ongkudon CM, Kansil T, Wong C
    J Sep Sci, 2014 Mar;37(5):455-64.
    PMID: 24376196 DOI: 10.1002/jssc.201300995
    To date, the number of published reports on the large-volume preparation of polymer-based monolithic chromatography adsorbents is still lacking and is of great importance. Many critical factors need to be considered when manufacturing a large-volume polymer-based monolith for chromatographic applications. Structural integrity, validity, and repeatability are thought to be the key factors determining the usability of a large-volume monolith in a separation process. In this review, we focus on problems and solutions pertaining to heat dissipation, pore size distribution, "wall channel" effect, and mechanical strength in monolith preparation. A template-based method comprising sacrificial and nonsacrificial techniques is possibly the method of choice due to its precise control over the porous structure. However, additional expensive steps are usually required for the template removal. Other strategies in monolith preparation are also discussed.
    Matched MeSH terms: Chromatography/instrumentation*
  2. Lim SR, Gooi BH, Singh M, Gam LH
    Appl Biochem Biotechnol, 2011 Nov;165(5-6):1211-24.
    PMID: 21863284 DOI: 10.1007/s12010-011-9339-3
    Limitation on two dimensional (2D) gel electrophoresis technique causes some proteins to be under presented, especially the extreme acidic, basic, or membrane proteins. To overcome the limitation of 2D electrophoresis, an analysis method was developed for identification of differentially expressed proteins in normal and cancerous colonic tissues using self-pack hydroxyapatite (HA) column. Normal and cancerous colon tissues were homogenized and proteins were extracted using sodium phosphate buffer at pH 6.8. Protein concentration was determined and the proteins were loaded unto the HA column. HA column reduced the complexity of proteins mixture by fractionating the proteins according to their ionic strength. Further protein separation was accomplished by a simple and cost effective sodium dodecyl sulfate-polyacrylamide gel electrophoresis method. The protein bands were subjected to in-gel digestion and protein analysis was performed using electrospray ionization (ESI) ion trap mass spectrometer. There were 17 upregulated proteins and seven downregulated proteins detected with significant differential expression. Some of these proteins were low abundant proteins or proteins with extreme pH that were usually under presented in 2D gel analysis. We have identified brain mitochondrial carrier protein 1, T-cell surface glycoprotein CD1a, SOSS complex subunit B2, and Protein Jade 1 which were previously not detected in 2D gel analysis method.
    Matched MeSH terms: Chromatography/instrumentation
Related Terms
Filters
Contact Us

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links