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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  EFFICIENT PRECIPITATION AND ACCURATE QUANTITATION OF DETERGENT-SOLUBILIZED MEMBRANE-PROTEINS


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48899


    Title: EFFICIENT PRECIPITATION AND ACCURATE QUANTITATION OF DETERGENT-SOLUBILIZED MEMBRANE-PROTEINS
    Authors: CHANG, YC
    教師: 張兗君
    Date: 1992
    Publisher: Elsevier
    Relation: Analytical Biochemistry,Elsevier,Volume 205,Issue 1,15 August 1992,Pages 22-26
    Keywords: GLUTAMATE BINDING-SITES
    PORCINE BRAIN
    LOWRY
    ACID
    Abstract: The protein assay method of [4.]) has been modified to provide a general method for quantitating protein samples in the presence of detergents. Dilute detergent-solubilized membrane proteins, by using ribonucleic acid as a carrier, have been efficiently precipitated here by trichloroacetic acid (TCA) in the presence of sodium dodecyl sulfate (SDS). Washing the pellets once with TCA solution has removed most of the reagents present in the original sample. The washed sample could then be quantitated by the Lowry method ( [1.]). This procedure could be used to assay protein solutions of a concentration as low as 5 μg/ml in the presence of the following reagents: Triton X-100, Triton X-114, Tween 20, N-octylglucoside, deoxycholate, cholate, Thesit, octanoyl-N-methylglucamide, isotridecylpoly (ethyleneglycoether)n, Nonidet P-40, glucose, methyl-D-glucopyranoside, methyl-D-mannopyranoside, N-acetyl-glucosamine, Mn2+, Ca2+, Mg2+, and many buffer reagents. Proteins solubilized from porcine brain myelin sheath and synaptic plasma membranes were quantitated by amino acid analysis and by the TCA/SDS precipitation method described here. The resultant protein concentrations were almost identical. The results have suggested this TCA/SDS precipitation method to be useful for quantitating dilute protein samples containing high concentrations of detergents and other reagents commonly employed in studying membrane proteins.
    URI: http://www.elsevier.com/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48899
    Appears in Collections:[生命科學系] 期刊論文

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