Eiwitzuiverheid

Eiwitzuiverheid refers to the degree to which a protein sample is free from other contaminating molecules. High protein purity is crucial for many biological and biochemical applications, including structural studies, enzymatic assays, and therapeutic protein production. Impurities can arise from various sources during protein isolation and purification, such as other cellular proteins, nucleic acids, lipids, or reagents used in the purification process.

Methods to assess protein purity typically involve separating the protein of interest from contaminants based on differences in their physical or chemical properties. Common techniques include sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), which separates proteins by size, and chromatography techniques like size exclusion chromatography (SEC), ion-exchange chromatography (IEC), and affinity chromatography. Spectroscopic methods, such as UV-Vis spectroscopy, can also provide an indication of purity by measuring the absorbance at specific wavelengths associated with proteins.

The acceptable level of purity depends on the intended use of the protein. For example, proteins used in structural biology may require extremely high purity to obtain well-ordered crystals for X-ray crystallography or to resolve fine details in nuclear magnetic resonance (NMR) spectroscopy. In contrast, some research applications might tolerate lower purity levels, provided the contaminants do not interfere with the specific experiment. Maintaining and verifying protein purity is a fundamental aspect of successful protein science and biotechnology.