Electrophoresis
Start with the big picture
Electrophoretic methods differ in how they separate molecules and what properties they preserve or measure. In gel electrophoresis, the matrix acts as a sieve: agarose and polyacrylamide provide different pore structures, and gel concentration affects fragment separation. SDS-PAGE gives proteins a uniform negative charge so separation reflects molecular weight, whereas native PAGE retains structure and activity. Isoelectric focusing separates proteins by their isoelectric point, and 2-D electrophoresis combines it with SDS-PAGE to resolve proteins by pI and size. Capillary electrophoresis offers rapid, high-resolution separations. Diagnostic examples include hemoglobin electrophoresis, serum protein electrophoresis, and immunofixation.
What you'll learn
- Explain how charge, size, shape, gel matrix, and buffer influence electrophoretic migration.
- Distinguish SDS-PAGE, native PAGE, isoelectric focusing, and two-dimensional electrophoresis.
- Describe the roles of capillary electrophoresis and nucleic acid gel methods.
- Identify examples of electrophoresis in hemoglobin and serum protein testing.
- Recognize how stains and size standards support band detection and estimation.
Continue your study
Work through the complete notes and reinforce the topic with the study tools available in the full lesson.
