Which method can reduce matrix effects during atomic absorption analysis?

Using protein-based calibrators can significantly reduce matrix effects during atomic absorption analysis because these calibrators are designed to mimic the sample matrix accurately. Matrix effects arise when components in a sample interfere with the measurement of the target analyte, leading to inaccurate results. Protein-based calibrators help to account for these interferences by mirroring the complex interactions within biological fluids like serum or plasma. By aligning the calibration curve with the sample's matrix composition, any alterations in the signal due to the matrix are minimized, improving the precision and accuracy of the results.

In contrast, utilizing a higher sample volume might increase the overall signal but does not necessarily account for matrix interferences and can instead amplify these effects if not appropriately managed. Relying solely on standard solutions may address the concentration of the analyte but will not reflect the actual sample's complexity, which can lead to misleading analytical results. Heating samples can cause degradation or loss of volatile components and may alter the sample matrix in unexpected ways, potentially introducing further variability rather than resolving the matrix effect. Thus, using protein-based calibrators provides a targeted approach to mitigate interferences in quantitative measurements in atomic absorption spectroscopy.