Biochemistry I Fall Term, 2004Gel Filtration and SDS PAGE GraphsThe two figures show calculated values for molecular seiving measurements.Fig. 1 Relative elution volume is plotted vs Mr (logarithmic scale) on a gel filtration column.The quaternary structure of some proteins we have studied in Biochemistry I:Protein Native Mr (Da) #SubunitsMyoglobin 17,200 1TIM (triosephosphate isomerase) 53,300 2Hemoglobin 62,000 4IgG (immunoglobulin G) 140,000 4ATCase (aspartate transcarbamoylase) 307,900 12Fig. 2 The monomer Mr (logarithmic scale) is plotted vs relative mobilities on SDS-PAGE.The proteins of Fig. 1 and their subunit molecular masses:Protein Subunit Mr (Da)IgG (heavy chain) 49,200ATCase (catalytic subunit) 34,300TIM (triosephosphate isomerase) 26,600IgG (light chain) 23,400Myoglobin 17,200ATCase (regultory subunit) 17,000Hemoglobin
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