A study of biochemical and physiological properties of normal and functionally impaired skeletal muscles
type: CreativeWork
description: The main aim of this study was to increase our understanding of the diversity and plasticity of skeletal muscle by using (i) normal and functionally impaired rat muscles from normotensive and spontaneously hypertensive rats, (ii) single, skinned fibre preparations, and (iii) a combination of biochemical [SDS-polyacrylamide gel electrophoresis (SDS-PAGE) analyses of Myosin Heavy Chain (MHC) isoform composition in single fibres and whole muscle homogenates] and physiological (single fibre measurements of contractile activation characteristics and caffeine thresholds for contraction) methods. From the beginning of this work it became clear, however, that the number of different protocols used for electrophoretic separation of MHC isoforms was almost as high as the number of studies using this method. Furthermore, all gel systems described so far in the literature proved to have a relatively low reproducibility in this and other laboratories. Finally, there was no published study in which the impact of changing different electrophoretic parameters on MHC isoform separation was examined in a systematic manner. Thus, some efforts had to be also directed towards closing this knowledge gap.
abstract: The main aim of this study was to increase our understanding of the diversity and plasticity of skeletal muscle by using (i) normal and functionally impaired rat muscles from normotensive and spontaneously hypertensive rats, (ii) single, skinned fibre preparations, and (iii) a combination of biochemical [SDS-polyacrylamide gel electrophoresis (SDS-PAGE) analyses of Myosin Heavy Chain (MHC) isoform composition in single fibres and whole muscle homogenates] and physiological (single fibre measurements of contractile activation characteristics and caffeine thresholds for contraction) methods. From the beginning of this work it became clear, however, that the number of different protocols used for electrophoretic separation of MHC isoforms was almost as high as the number of studies using this method. Furthermore, all gel systems described so far in the literature proved to have a relatively low reproducibility in this and other laboratories. Finally, there was no published study in which the impact of changing different electrophoretic parameters on MHC isoform separation was examined in a systematic manner. Thus, some efforts had to be also directed towards closing this knowledge gap.
author: Bortolotto, Susan Kate
language: en
keywords: 0606 Physiology, 0601 Biochemistry and Cell Biology, School of Biomedical and Health Sciences
date published: 2000
date modified: 2026-07-24T06:33:12Z
provider: Victoria University (Australia)
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Victoria University of Technology