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Electron Microscopic Observations of Rabbit Antibodies

Electron micrographs were obtained showing the individual, shadow-cast macromolecules from solutions of purified anti-p-azobenzoate rabbit antibody and of normal γ-globulin. The two materials look alike and consist mainly of asymmetrical rod-like particles about 30 to 40 A in diameter. Lengths are n...

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Detalles Bibliográficos
Autores principales: Hall, C. E., Nisonoff, A., Slayter, H. S.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1959
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224689/
https://www.ncbi.nlm.nih.gov/pubmed/19866560
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author Hall, C. E.
Nisonoff, A.
Slayter, H. S.
author_facet Hall, C. E.
Nisonoff, A.
Slayter, H. S.
author_sort Hall, C. E.
collection PubMed
description Electron micrographs were obtained showing the individual, shadow-cast macromolecules from solutions of purified anti-p-azobenzoate rabbit antibody and of normal γ-globulin. The two materials look alike and consist mainly of asymmetrical rod-like particles about 30 to 40 A in diameter. Lengths are not constant but the weight average is about 250 A for the antibodies and about 200 A for the γ-globulin. The average observed dimensions are reasonably consistent with values deduced from physical-chemical methods, although the shape is more nearly that of a cylindrical rod rather than the ellipsoid employed in hydrodynamical theory. Mixtures of antibody and specific dihaptenic dye were examined in attempts to establish the mode of the specific aggregation. At the high dilutions necessary for electron microscopy (0.1 mg./ml.), the effect of the dye was small and tended to be masked by non-specific aggregation on drying. The evidence suggests that under these conditions the specific reaction involves an end-to-end aggregation of the elementary particles to produce a weight average length about twice that of the pure antibody.
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spelling pubmed-22246892008-05-01 Electron Microscopic Observations of Rabbit Antibodies Hall, C. E. Nisonoff, A. Slayter, H. S. J Biophys Biochem Cytol Article Electron micrographs were obtained showing the individual, shadow-cast macromolecules from solutions of purified anti-p-azobenzoate rabbit antibody and of normal γ-globulin. The two materials look alike and consist mainly of asymmetrical rod-like particles about 30 to 40 A in diameter. Lengths are not constant but the weight average is about 250 A for the antibodies and about 200 A for the γ-globulin. The average observed dimensions are reasonably consistent with values deduced from physical-chemical methods, although the shape is more nearly that of a cylindrical rod rather than the ellipsoid employed in hydrodynamical theory. Mixtures of antibody and specific dihaptenic dye were examined in attempts to establish the mode of the specific aggregation. At the high dilutions necessary for electron microscopy (0.1 mg./ml.), the effect of the dye was small and tended to be masked by non-specific aggregation on drying. The evidence suggests that under these conditions the specific reaction involves an end-to-end aggregation of the elementary particles to produce a weight average length about twice that of the pure antibody. The Rockefeller University Press 1959-12-01 /pmc/articles/PMC2224689/ /pubmed/19866560 Text en Copyright © Copyright, 1959, by The Rockefeller Institute
spellingShingle Article
Hall, C. E.
Nisonoff, A.
Slayter, H. S.
Electron Microscopic Observations of Rabbit Antibodies
title Electron Microscopic Observations of Rabbit Antibodies
title_full Electron Microscopic Observations of Rabbit Antibodies
title_fullStr Electron Microscopic Observations of Rabbit Antibodies
title_full_unstemmed Electron Microscopic Observations of Rabbit Antibodies
title_short Electron Microscopic Observations of Rabbit Antibodies
title_sort electron microscopic observations of rabbit antibodies
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224689/
https://www.ncbi.nlm.nih.gov/pubmed/19866560
work_keys_str_mv AT hallce electronmicroscopicobservationsofrabbitantibodies
AT nisonoffa electronmicroscopicobservationsofrabbitantibodies
AT slayterhs electronmicroscopicobservationsofrabbitantibodies