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SHR Neuro Cancer Cardio Lipid Metab Microb

Habisch, H; Zhang, F; Zhou, Q; Madl, T.
Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy.
JOVE-J VIS EXP. 2021; (178): Doi: 10.3791/63245
Web of Science PubMed FullText FullText_MUG

Leading authors Med Uni Graz: Habisch Hansjörg; Madl Tobias; Zhang Fangrong
Co-authors Med Uni Graz: Zhou Qishun
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Abstract:: Protein-bound arginine is commonly methylated in many proteins and regulates their function by altering the physicochemical properties, their interaction with other molecules, including other proteins or nucleic acids. This work presents an easily implementable protocol for quantifying arginine and its derivatives, including asymmetric and symmetric dimethylarginine (ADMA and SDMA, respectively) and monomethyl arginine (MMA). Following protein isolation from biological body fluids, tissues, or cell lysates, a simple method for homogenization, precipitation of proteins, and protein hydrolysis is described. Since the hydrolysates contain many other components, such as other amino acids, lipids, and nucleic acids, a purification step using solid-phase extraction (SPE) is essential. SPE can either be performed manually using centrifuges or a pipetting robot. The sensitivity for ADMA using the current protocol is about 100 nmol/L. The upper limit of detection for arginine is 3 mmol/L due to SPE saturation. In summary, this protocol describes a robust method, which spans from biological sample preparation to NMR-based detection, providing valuable hints and pitfalls for successful work when studying the arginine methylome.
Find related publications in this database (using NLM MeSH Indexing): Arginine - chemistry; Epigenome - administration & dosage; Magnetic Resonance Spectroscopy - administration & dosage; Reproducibility of Results - administration & dosage; Solid Phase Extraction - administration & dosage