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Related Concept Videos

Precipitation Gravimetry01:03

Precipitation Gravimetry

7.5K
Precipitation gravimetry is based on converting an analyte into a sparingly soluble precipitate, which is separated by filtration and weighed. An ideal precipitate should be pure, insoluble, of known composition, and easily filtered from the reaction mixture.
In determining nickel by gravimetric analysis, a precipitant of ethanolic dimethylglyoxime is added to a hot nickel salt solution. This is quickly followed by the dropwise addition of dilute ammonia solution until precipitation occurs. A...
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Washing, Drying, and Ignition of Precipitates00:52

Washing, Drying, and Ignition of Precipitates

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After filtration, the precipitate is washed to remove coprecipitated impurities and any remaining mother liquor. Colloidal precipitates, such as silver chloride, are washed with an electrolyte (such as dilute nitric acid) to prevent the peptization of the precipitate. In the case of slightly soluble precipitates, the wash solution contains a common ion to reduce solubility. Lead sulfate, which is slightly soluble in water, is washed with dilute sulfuric acid. Similarly, wash solutions may be...
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Updated: Sep 13, 2025

Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry
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Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry

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ZnCl2 Precipitation-Assisted Sample Preparation for Proteomic Analysis.

Qiqing He1,2,3, Qingjing Chen2,3,4, Dongxue Wang2,3,5

  • 1Department of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, China.

Bio-Protocol
|July 31, 2025
PubMed
Summary
This summary is machine-generated.

ZnCl2 precipitation-assisted sample preparation (ZASP) offers a cost-effective and efficient method for proteomic analysis. This protocol effectively removes impurities and recovers over 90% of proteins, outperforming other sample preparation techniques.

Keywords:
LC–MS-incompatible reagentsProtein recoveryProteomics.Sample preparationZnCl2 induced protein precipitation

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Area of Science:

  • Proteomics and Mass Spectrometry
  • Biochemistry and Molecular Biology

Background:

  • Traditional proteomic sample preparation methods often struggle with removing detergents and impurities, impacting protein recovery and analysis sensitivity.
  • Harsh chemicals like sodium dodecyl sulfate (SDS) and urea are common in biological lysates but interfere with downstream enzymatic digestion and mass spectrometry.
  • Developing robust, cost-effective, and efficient sample preparation protocols is crucial for advancing proteomic research.

Purpose of the Study:

  • To introduce and validate the ZnCl2 precipitation-assisted sample preparation (ZASP) protocol for enhanced proteomic analysis.
  • To demonstrate ZASP's effectiveness in removing common contaminants and improving protein recovery.
  • To compare ZASP's performance against established sample preparation methods.

Main Methods:

  • Proteins were precipitated using ZASP precipitation buffer (ZPB), containing ZnCl2 and methanol, to remove detergents and impurities.
  • Protein recovery rates were assessed by incubating lysates with ZPB.
  • Proteomic analysis was performed using data-dependent acquisition (DDA) on an Exploris 480 mass spectrometer.
  • ZASP performance was benchmarked against sodium deoxycholate (SDC)-based digestion, acetone precipitation, filter-aided sample preparation (FASP), and single-pot, solid-phase-enhanced sample preparation (SP3).

Main Results:

  • ZASP achieved over 90% protein recovery from lysates within 10 minutes at room temperature.
  • Analysis of 1 μg of mouse small intestine proteins yielded 4,037 proteins and 25,626 peptides, with higher yields for increased input.
  • ZASP outperformed other methods in protein and peptide identification, achieving 4,456 proteins and 29,871 peptides, with lower missing cleavage rates (16.3%) and high reproducibility (Pearson correlation coefficient of 0.96).
  • The cost per sample for ZASP is less than 30 RMB, including trypsin.

Conclusions:

  • ZASP is a user-friendly, efficient, sensitive, and cost-effective method for proteomic sample preparation suitable for standard biochemistry labs.
  • The protocol enables high protein recovery and unbiased analysis from diverse biological samples, including cells and tissues (OCT-embedded and FFPE).
  • ZASP significantly improves proteomic data quality and reproducibility compared to conventional methods.