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Related Concept Videos

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...
Immunogold Electron Microscopy01:20

Immunogold Electron Microscopy

Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.

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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
20:23

A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples

Published on: October 1, 2009

Glycoprotein enrichment through lectin affinity techniques.

Yehia Mechref1, Milan Madera, Milos V Novotny

  • 1Indiana University, Bloomington, Indiana, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 29, 2008
PubMed
Summary
This summary is machine-generated.

Posttranslational modifications (PTM) significantly expand protein functions. Lectin affinity chromatography is crucial for isolating glycoproteins, essential for discovering disease biomarkers in complex biological samples.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Glycomics

Background:

  • Posttranslational modifications (PTM) are vital for protein function, activity, localization, and interaction, especially given the limited number of human genes.
  • Glycosylation affects approximately 50% of all proteins, highlighting its critical physiological role in mammals.
  • Aberrant glycosylation is linked to various diseases, including cancer and neurodegenerative disorders, underscoring the need for studying glycoproteins.

Purpose of the Study:

  • To review and describe lectin affinity chromatography methods for glycoprotein enrichment.
  • To emphasize the importance of glycoprotein isolation for biomarker discovery in complex biological samples.
  • To present lectin affinity chromatography in various formats for proteomic and glycomic studies.

Main Methods:

  • Immobilized lectins are the primary tool for selective glycoprotein enrichment.
  • Lectin affinity chromatography is employed in diverse formats, including tubes, packed columns, and microfluidic channels.
  • These methods facilitate the isolation of glycoproteins from complex biological matrices.

Main Results:

  • Lectin affinity chromatography enables the selective enrichment of glycoproteins.
  • Various formats of lectin affinity chromatography are available for different research needs.
  • The described methods are critical for advancing proteomic and glycomic analyses.

Conclusions:

  • Glycoprotein enrichment using lectin affinity chromatography is essential for identifying disease biomarkers.
  • The described methodologies support in-depth proteomic and glycomic investigations.
  • Advancements in glycoprotein isolation techniques are crucial for understanding health and disease.