This document introduces the effect of temperature on protein size exclusion chromatography
Proteins are often unstable outside their native environment, with conditions like temperature significantly impacting their function. This document explores the effect of varying temperatures on globular proteins to identify unfolded or aggregated species.
The study analyzes y-globulins, BSA, and ovalbumin using Agilent ProSEC columns at temperatures ranging from 5 °C to 65 °C. Results indicate that while lower temperatures maintain stability for some proteins, higher temperatures cause significant aggregation and shifts in elution behavior, particularly for ovalbumin.
The analysis was conducted at four specific temperatures: 5 °C, 25 °C, 45 °C, and 65 °C.
The experiment utilized a constant flow rate of 1.0 mL/min.
The detector was set to measure UV intensity at a wavelength of 310 nm.