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Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state
Instrumentation has been developed to detect rapidly the polarization of tryptophan fluorescence from single muscle fibers in rigor, relaxation, and contraction. The polarization parameter (P(⊥)) obtained by exiciting the muscle tryptophans with light polarized perpendicular to the long axis of the...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1972
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213788/ https://www.ncbi.nlm.nih.gov/pubmed/4332133 |
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author | dos Remedios, C. G. Millikan, R. G. C. Morales, M. F. |
author_facet | dos Remedios, C. G. Millikan, R. G. C. Morales, M. F. |
author_sort | dos Remedios, C. G. |
collection | PubMed |
description | Instrumentation has been developed to detect rapidly the polarization of tryptophan fluorescence from single muscle fibers in rigor, relaxation, and contraction. The polarization parameter (P(⊥)) obtained by exiciting the muscle tryptophans with light polarized perpendicular to the long axis of the muscle fiber had a magnitude P(⊥) (relaxation) > P(⊥) (contraction) > P(⊥) (rigor) for the three types of muscle fibers examined (glycerinated rabbit psoas, glycerinated dorsal longitudinal flight muscle of Lethocerus americanus, and live semitendinosus of Rana pipiens). P(⊥) from single psoas fibers in rigor was found to increase as the sarcomere length increased but in relaxed fibers P(⊥) was independent of sarcomere length. After rigor, pyrophosphate produced little or no change in P(⊥), but following an adenosine triphosphate (ATP)-containing solution, pyrophosphate produced a value of P(⊥) that fell between the contraction and relaxation values. Sinusoidal or square wave oscillations of the muscle of amplitude 0.5–2.0% of the sarcomere length and frequency 1, 2, or 5 Hz were applied in rigor when the myosin cross-bridges are considered to be firmly attached to the thin filaments. No significant changes in P(⊥) were observed in either rigor or relaxation. The preceding results together with our present knowledge of tryptophan distribution in the contractile proteins has led us to the conclusion that the parameter P(⊥) is a probe of the contractile state of myosin which is probably sensitive to the orientation of the myosin S1 subfragment. |
format | Text |
id | pubmed-2213788 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1972 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22137882008-04-23 Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state dos Remedios, C. G. Millikan, R. G. C. Morales, M. F. J Gen Physiol Article Instrumentation has been developed to detect rapidly the polarization of tryptophan fluorescence from single muscle fibers in rigor, relaxation, and contraction. The polarization parameter (P(⊥)) obtained by exiciting the muscle tryptophans with light polarized perpendicular to the long axis of the muscle fiber had a magnitude P(⊥) (relaxation) > P(⊥) (contraction) > P(⊥) (rigor) for the three types of muscle fibers examined (glycerinated rabbit psoas, glycerinated dorsal longitudinal flight muscle of Lethocerus americanus, and live semitendinosus of Rana pipiens). P(⊥) from single psoas fibers in rigor was found to increase as the sarcomere length increased but in relaxed fibers P(⊥) was independent of sarcomere length. After rigor, pyrophosphate produced little or no change in P(⊥), but following an adenosine triphosphate (ATP)-containing solution, pyrophosphate produced a value of P(⊥) that fell between the contraction and relaxation values. Sinusoidal or square wave oscillations of the muscle of amplitude 0.5–2.0% of the sarcomere length and frequency 1, 2, or 5 Hz were applied in rigor when the myosin cross-bridges are considered to be firmly attached to the thin filaments. No significant changes in P(⊥) were observed in either rigor or relaxation. The preceding results together with our present knowledge of tryptophan distribution in the contractile proteins has led us to the conclusion that the parameter P(⊥) is a probe of the contractile state of myosin which is probably sensitive to the orientation of the myosin S1 subfragment. The Rockefeller University Press 1972-01-01 /pmc/articles/PMC2213788/ /pubmed/4332133 Text en Copyright © 1972 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/). |
spellingShingle | Article dos Remedios, C. G. Millikan, R. G. C. Morales, M. F. Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state |
title | Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state |
title_full | Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state |
title_fullStr | Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state |
title_full_unstemmed | Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state |
title_short | Polarization of Tryptophan Fluorescence from Single Striated Muscle Fibers : A molecular probe of contractile state |
title_sort | polarization of tryptophan fluorescence from single striated muscle fibers : a molecular probe of contractile state |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213788/ https://www.ncbi.nlm.nih.gov/pubmed/4332133 |
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