THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES

Spectrin, a major protein constituent of mammalian red blood cell membrane preparations, has been localized on the inner surface of human red blood cell membranes by techniques that utilized specific ferritin-conjugated antibodies and fixation of membranes shortly after hemolysis so as to allow pen...

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Main Authors: Nicolson, Garth L., Marchesi, V. T., Singer, S. J.
Format: Online
Language:English
Published: The Rockefeller University Press 1971
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108256/
id pubmed-2108256
recordtype oai_dc
spelling pubmed-21082562008-05-01 THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES Nicolson, Garth L. Marchesi, V. T. Singer, S. J. Article Spectrin, a major protein constituent of mammalian red blood cell membrane preparations, has been localized on the inner surface of human red blood cell membranes by techniques that utilized specific ferritin-conjugated antibodies and fixation of membranes shortly after hemolysis so as to allow penetration of the ferritin-antibody labels. The labeling of spectrin was shown to be specific by the following criteria. (a) Nonhomologous ferritin-conjugated antibodies did not specifically bind to either membrane surface. (b) Blocking the membrane-bound spectrin with excess unconjugated antispectrin antibodies prevented ferritin-antibody labeling. (c) Removal of spectrin by treating the membrane preparation with a low ionic strength buffer containing ethylenediaminetetraacetate and β-mercaptoethanol prevented labeling by specific ferritin-conjugated antibodies. The Rockefeller University Press 1971-10-01 /pmc/articles/PMC2108256/ /pubmed/5000071 Text en Copyright © 1971 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Nicolson, Garth L.
Marchesi, V. T.
Singer, S. J.
spellingShingle Nicolson, Garth L.
Marchesi, V. T.
Singer, S. J.
THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES
author_facet Nicolson, Garth L.
Marchesi, V. T.
Singer, S. J.
author_sort Nicolson, Garth L.
title THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES
title_short THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES
title_full THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES
title_fullStr THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES
title_full_unstemmed THE LOCALIZATION OF SPECTRIN ON THE INNER SURFACE OF HUMAN RED BLOOD CELL MEMBRANES BY FERRITIN-CONJUGATED ANTIBODIES
title_sort localization of spectrin on the inner surface of human red blood cell membranes by ferritin-conjugated antibodies
description Spectrin, a major protein constituent of mammalian red blood cell membrane preparations, has been localized on the inner surface of human red blood cell membranes by techniques that utilized specific ferritin-conjugated antibodies and fixation of membranes shortly after hemolysis so as to allow penetration of the ferritin-antibody labels. The labeling of spectrin was shown to be specific by the following criteria. (a) Nonhomologous ferritin-conjugated antibodies did not specifically bind to either membrane surface. (b) Blocking the membrane-bound spectrin with excess unconjugated antispectrin antibodies prevented ferritin-antibody labeling. (c) Removal of spectrin by treating the membrane preparation with a low ionic strength buffer containing ethylenediaminetetraacetate and β-mercaptoethanol prevented labeling by specific ferritin-conjugated antibodies.
publisher The Rockefeller University Press
publishDate 1971
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2108256/
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