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Related Concept Videos

Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors01:30

Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors

Angiotensin-converting enzyme (ACE), a vital component of the renin-angiotensin-aldosterone system, is abundant in lung endothelial cells. ACE converts the inactive decapeptide, angiotensin I, into the active octapeptide, angiotensin II. This potent vasoconstrictor narrows blood vessels, increasing resistance to blood flow and elevating blood pressure. Angiotensin II also stimulates aldosterone production, encouraging kidney cells to reabsorb more sodium and water from urine, thereby increasing...
Immunoprecipitation01:20

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: May 16, 2026

Peptide and Protein Quantification Using Automated Immuno-MALDI (iMALDI)
08:57

Peptide and Protein Quantification Using Automated Immuno-MALDI (iMALDI)

Published on: August 18, 2017

Automated multi-step purification protocol for Angiotensin-I-Converting-Enzyme (ACE).

Thomas Eisele1, Timo Stressler, Bertolt Kranz

  • 1University of Hohenheim, Institute of Food Science and Biotechnology, Department of Biotechnology, Garbenstr. 25, 70599 Stuttgart, Germany. t.eisele@uni-hohenheim.de

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
|December 11, 2012
PubMed
Summary

Automated purification of Angiotensin-I-Converting-Enzyme (ACE) from pig lung was achieved in under 8 hours. This efficient method yields highly purified ACE with significant specific activity, adaptable for other proteins.

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Nitropeptide Profiling and Identification Illustrated by Angiotensin II
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Published on: June 16, 2019

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Enzymology

Background:

  • High-purity proteins are crucial for biochemical and functional studies.
  • Traditional protein purification methods are often lengthy and labor-intensive.
  • Angiotensin-I-Converting-Enzyme (ACE) purification typically involves detergents and multiple steps.

Purpose of the Study:

  • To develop an automated, rapid purification protocol for Angiotensin-I-Converting-Enzyme (ACE).
  • To achieve high ACE purity and specific activity without using common detergents.
  • To demonstrate the adaptability of the automated protocol for other protein purification challenges.

Main Methods:

  • Solubilization of ACE from pig lung under mild alkaline conditions (pH 9.0) without detergents.
  • Automation using a fast-protein-liquid-chromatography (FPLC) system with switching valves for buffer stream inversion and protein parking.
  • A four-step chromatography process including hydrophobic interaction and anion exchange chromatography, with two desalting steps.
  • Characterization using SDS-PAGE and native PAGE with a novel activity staining protocol employing l-Phe-Gly-Gly substrate.

Main Results:

  • Automated ACE purification completed in less than 8 hours.
  • Achieved a purification factor of 308 with a specific activity of 37 U/mg and a yield of 23.6%.
  • Determined monomeric ACE size as ~175 kDa and dimeric form as ~330 kDa via SDS-PAGE and native PAGE, respectively.

Conclusions:

  • The developed automated protocol significantly reduces ACE purification time.
  • The method provides high purity and specific activity without detergents, offering a more efficient alternative.
  • The protocol's design allows for straightforward adaptation to purify other proteins.