High Mass Calibration Using Protein Histidine Phosphatase
Author Information
Author(s): Ludwig Katrin, Habbach Schähdi, Krieglstein Josef, Klumpp Susanne, König Simone
Primary Institution: University of Münster, Germany
Hypothesis
Can recombinant human 16 kDa protein histidine phosphatase be used as a calibration standard for high mass ranges in mass spectrometry?
Conclusion
The study concludes that PHP can be produced with high quality and serves as a valuable calibration compound for high mass ranges above 100 kDa.
Supporting Evidence
- PHP forms multimers consisting of up to more than 35 protein molecules.
- In MALDI-TOF MS, PHP generates adduct ions every 16 kDa.
- PHP can be produced with high quality, making it a feasible calibration compound.
Takeaway
Researchers found that a special protein can help measure very large proteins in experiments, making it easier to get accurate results.
Methodology
The study involved gel filtration analysis and MALDI-TOF mass spectrometry to observe PHP aggregation and calibration capabilities.
Limitations
The study did not determine whether PHP activity was due to the monomer or one of the aggregate forms.
Digital Object Identifier (DOI)
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