Gel Electrophoresis In a native PAGE, proteins are separated on the basis of net positive charge net negative charge net positive charges size net charge and size net positive charge net negative charge net positive charges size net charge and size ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis In isoelectric focusing, proteins are separated on the basis of their relative content of positively charged residue only size relative content of positively and negatively charged residue relative content of negatively charged residue only relative content of positively charged residue only size relative content of positively and negatively charged residue relative content of negatively charged residue only ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in both proteins migrate to the cathode histones migrate to the anode and myoglobin migrates to the cathode histones migrate to the cathode and myoglobin migrates to the anode both proteins migrate to the anode both proteins migrate to the cathode histones migrate to the anode and myoglobin migrates to the cathode histones migrate to the cathode and myoglobin migrates to the anode both proteins migrate to the anode ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis In an SDS-PAGE proteins have the same charge-to-mass ratio proteins are denatured by the SDS All of these smaller proteins migrate more rapidly through the gel proteins have the same charge-to-mass ratio proteins are denatured by the SDS All of these smaller proteins migrate more rapidly through the gel ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis The subunit molecular weight as well as the number of subunits in the quaternary structure can be determined by isoelectric focusing SDS-PAGE electrophoresis gel filtration chromatography combining information from (a)and (b) isoelectric focusing SDS-PAGE electrophoresis gel filtration chromatography combining information from (a)and (b) ANSWER DOWNLOAD EXAMIANS APP
Gel Electrophoresis In SDS-PAGE, the protein sample is first treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent. None of these treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent. None of these ANSWER DOWNLOAD EXAMIANS APP
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