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Jennison, Katy
(1992).
DOI: https://doi.org/10.21954/ou.ro.00010165
Abstract
In this study, muscle proteins were extracted, and concentrated gels of these proteins were produced. Microelectrode techniques were developed in order to measure the electrical charge in these gels.
Results of the charge measurements confirm that myosin and actin, respectively, are the principle contributors of the charge found in the A- and I-bands of intact muscle fibres. Results also generally accord with the charge predicted by the amino-acid composition of these proteins. However, the charge on myosin in particular is lower than that found in the A-band.
Myosin charge was measured under a variety of experimental conditions. Only in combination with C-protein did the charge approach that found in intact muscle.
Gels of F-actin were measured at both high and low concentrations. The low-concentration gel (23-75 mg/ml) was found to change charge upon stirring. Further work is indicated to elucidate this phenomenon.
The results of this study suggest that variations in charge may be related principally to two factors. First, conformational changes in the protein molecule are likely to affect ion binding. Second, different experimental conditions and protein combinations are likely to affect the degree of order of the protein gel.
CORE (COnnecting REpositories)
CORE (COnnecting REpositories)
