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Measurement of Globular Protein Molecules by Electron Microscopy

A series of molecular species with approximately spherical shape and with molecular weights between 35,000 and 250,000 were shadowed with platinum while resting on a cleaved mica surface. They were backed, stripped from the surface, and examined by electron microscopy. Materials examined were: pepsi...

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Detalles Bibliográficos
Autor principal: Hall, Cecil E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1960
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224881/
https://www.ncbi.nlm.nih.gov/pubmed/14399016
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author Hall, Cecil E.
author_facet Hall, Cecil E.
author_sort Hall, Cecil E.
collection PubMed
description A series of molecular species with approximately spherical shape and with molecular weights between 35,000 and 250,000 were shadowed with platinum while resting on a cleaved mica surface. They were backed, stripped from the surface, and examined by electron microscopy. Materials examined were: pepsin, liver alcohol dehydrogenase, yeast alcohol dehydrogenase, glutamic dehydrogenase, polyhedral virus protein (insect), fibrinogen substructure, alkaline phosphatase, and microsomal particles from Escherichia coli. Measurements were made of widths perpendicular to the shadowing direction and heights were deduced from shadow lengths. For those molecular species with well established molecular weights the average heights correlate very well with the diameter of the theoretical sphere but the average widths are too great by 50 to 80 A due to the lateral growth of the deposited metal. Although the distortion in shape of shadowed particles is relatively large, with standardized conditions for shadowing, it is possible to make allowance for the distortion and to obtain reasonably reliable estimates of the dimensions of spherical organic particles down to a molecular weight of about 35,000.
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spelling pubmed-22248812008-05-01 Measurement of Globular Protein Molecules by Electron Microscopy Hall, Cecil E. J Biophys Biochem Cytol Article A series of molecular species with approximately spherical shape and with molecular weights between 35,000 and 250,000 were shadowed with platinum while resting on a cleaved mica surface. They were backed, stripped from the surface, and examined by electron microscopy. Materials examined were: pepsin, liver alcohol dehydrogenase, yeast alcohol dehydrogenase, glutamic dehydrogenase, polyhedral virus protein (insect), fibrinogen substructure, alkaline phosphatase, and microsomal particles from Escherichia coli. Measurements were made of widths perpendicular to the shadowing direction and heights were deduced from shadow lengths. For those molecular species with well established molecular weights the average heights correlate very well with the diameter of the theoretical sphere but the average widths are too great by 50 to 80 A due to the lateral growth of the deposited metal. Although the distortion in shape of shadowed particles is relatively large, with standardized conditions for shadowing, it is possible to make allowance for the distortion and to obtain reasonably reliable estimates of the dimensions of spherical organic particles down to a molecular weight of about 35,000. The Rockefeller University Press 1960-07-01 /pmc/articles/PMC2224881/ /pubmed/14399016 Text en Copyright © Copyright, 1960, by The Rockefeller Institute Press
spellingShingle Article
Hall, Cecil E.
Measurement of Globular Protein Molecules by Electron Microscopy
title Measurement of Globular Protein Molecules by Electron Microscopy
title_full Measurement of Globular Protein Molecules by Electron Microscopy
title_fullStr Measurement of Globular Protein Molecules by Electron Microscopy
title_full_unstemmed Measurement of Globular Protein Molecules by Electron Microscopy
title_short Measurement of Globular Protein Molecules by Electron Microscopy
title_sort measurement of globular protein molecules by electron microscopy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2224881/
https://www.ncbi.nlm.nih.gov/pubmed/14399016
work_keys_str_mv AT hallcecile measurementofglobularproteinmoleculesbyelectronmicroscopy