**Title: Understanding Contaminant Proteins in LDH Fraction After Purification****Question:**If there are still contaminating proteins in your LDH (Lactate Dehydrogenase) fraction after going through three different purification schemes (affinity, ion exchange, and size exclusion columns), what would be their physical characteristics?**Explanation:**After subjecting your LDH fraction to three purification methods, ideally, contaminants should have been removed. However, if they persist, they likely possess similar physical characteristics to LDH, making them difficult to separate. Below are explanations of each purification scheme and potential reasons for contamination.**1. Affinity Chromatography:** - **Principle:** Relies on the specific binding affinity between a protein and a particular ligand. - **Potential Issues:** Contaminants may share a similar affinity for the ligand used, resulting in co-elution with LDH.**2. Ion Exchange Chromatography:** - **Principle:** Separates proteins based on their net charge by using a charged resin. - **Potential Issues:** Contaminants may have similar charge properties to LDH under the chosen pH and ionic strength conditions, leading to incomplete separation.**3. Size Exclusion Chromatography (SEC):** - **Principle:** Separates proteins based on size as they pass through a column filled with porous beads. - **Potential Issues:** Proteins of similar molecular size may remain inseparable from LDH, as SEC does not distinguish between proteins of similar sizes or native conformations.**Conclusion:**Understanding the characteristics of contaminants is essential. They likely share specific binding, charge, or size properties with LDH, complicating their removal. Further purification strategies may involve adjusting pH, ionic conditions, or using more specific affinity tags.

Proteins are high molecular weight biomolecules made up of amino acid residues linked via peptide…

Answered: If there are still contaminating…

Biochemistry

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Chapter1: Biochemistry: An Evolving Science

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If there are still contaminating proteins with your LDH fraction after going through 3 different purification schemes (affinity, ion exchange, and size exclusion columns), what would be their physical characteristics?