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An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins

We elicited antibodies in rabbits to actin purified from body wall muscle of the marine mollusc, Aplysia californica. We found that this antiactin has an unusual specificity: in addition to reacting with the immunogen, it recognizes cytoplasmic vertebrate actins but not myofibrillar actin. Radioimmu...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1980
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110679/
https://www.ncbi.nlm.nih.gov/pubmed/6893333
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collection PubMed
description We elicited antibodies in rabbits to actin purified from body wall muscle of the marine mollusc, Aplysia californica. We found that this antiactin has an unusual specificity: in addition to reacting with the immunogen, it recognizes cytoplasmic vertebrate actins but not myofibrillar actin. Radioimmunoassay showed little or no cross-reaction with actin purified from either chicken gizzard or rabbit skeletal muscle. Immunocytochemical studies with human fibroblasts and L6 myoblasts revealed intense staining of typical cytoplasmic cables. Myofibrils were not stained after treatment of human and frog skeletal muscle with the antibody, although the distribution of immunofluorescence suggested that cytoplasmic actin is associated with membrane systems in the muscle fiber. The antibody may therefore be especially suited for studying the localization of cytoplasmic actin in skeletal muscle cells even in the presence of a great excess of the myofibrillar form.
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spelling pubmed-21106792008-05-01 An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins J Cell Biol Articles We elicited antibodies in rabbits to actin purified from body wall muscle of the marine mollusc, Aplysia californica. We found that this antiactin has an unusual specificity: in addition to reacting with the immunogen, it recognizes cytoplasmic vertebrate actins but not myofibrillar actin. Radioimmunoassay showed little or no cross-reaction with actin purified from either chicken gizzard or rabbit skeletal muscle. Immunocytochemical studies with human fibroblasts and L6 myoblasts revealed intense staining of typical cytoplasmic cables. Myofibrils were not stained after treatment of human and frog skeletal muscle with the antibody, although the distribution of immunofluorescence suggested that cytoplasmic actin is associated with membrane systems in the muscle fiber. The antibody may therefore be especially suited for studying the localization of cytoplasmic actin in skeletal muscle cells even in the presence of a great excess of the myofibrillar form. The Rockefeller University Press 1980-09-01 /pmc/articles/PMC2110679/ /pubmed/6893333 Text en 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/).
spellingShingle Articles
An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
title An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
title_full An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
title_fullStr An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
title_full_unstemmed An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
title_short An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
title_sort antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actins
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110679/
https://www.ncbi.nlm.nih.gov/pubmed/6893333