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Immunogold Electron Microscopy

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.

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

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Obtaining High-Quality Cryosections of Whole Rabbit Eye

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Electron Microscopic Observations of Rabbit Antibodies.

C E Hall¹, A Nisonoff, H S Slayter

¹Department of Biology, Massachusetts Institute of Technology, and the Roswell Park Memorial Institute, Buffalo.

The Journal of Biophysical and Biochemical Cytology

|October 30, 2009

Summary

This summary is machine-generated.

Rabbit antibodies and normal gamma-globulin appear as rod-like particles. Specific dye binding suggests end-to-end aggregation of antibody particles, potentially doubling their length.

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Area of Science:

Immunology and Structural Biology
Macromolecular structure determination

Background:

Understanding the molecular structure of antibodies is crucial for elucidating their function.
Previous studies utilized physical-chemical methods to infer antibody dimensions.

Purpose of the Study:

To visualize and characterize the structure of purified rabbit antibodies and normal gamma-globulin using electron microscopy.
To investigate the aggregation behavior of antibodies upon binding with a specific dihaptenic dye.

Main Methods:

Preparation of shadow-cast electron micrographs of purified anti-p-azobenzoate rabbit antibody and normal gamma-globulin.
Examination of antibody-dye mixtures under electron microscopy at high dilutions (0.1 mg./ml.).

Main Results:

Both antibody and gamma-globulin presented as asymmetrical, rod-like particles (30-40 A diameter).
Weight-average lengths were approximately 250 A for antibodies and 200 A for gamma-globulin.
Specific dye binding showed a tendency for end-to-end aggregation of antibody particles, increasing average length.

Conclusions:

Electron microscopy reveals rod-like structures for rabbit antibodies and gamma-globulin, consistent with physical-chemical data.
Observed dimensions favor a cylindrical rod model over an ellipsoid for these macromolecules.
Specific antibody-dye interactions likely involve end-to-end aggregation, though non-specific aggregation can occur.