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Speeds of Actin Translocation in Vitro by Myosins Extracted from Single Rat Muscle Fibres of Different Types
Author(s) -
Canepari M.,
Rossi R.,
Pellegrino M. A.,
Reggiani C.,
Bottinelli R.
Publication year - 1999
Publication title -
experimental physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.925
H-Index - 101
eISSN - 1469-445X
pISSN - 0958-0670
DOI - 10.1111/j.1469-445x.1999.00350.x
Subject(s) - myosin , gene isoform , actin , skeletal muscle , in vitro , myosin light chain kinase , motility , microbiology and biotechnology , chemistry , biophysics , biochemistry , biology , anatomy , gene
SUMMARY As skeletal muscle fibres mostly express a single myosin isoform, they are a potential source of pure myosin isoforms. A technique is described that allows extraction and identification of pure myosin isoforms from single fibres, and testing of such myosins in an in vitro motility assay (IVMA). The results show that the extraction procedure does not alter myosin function and support the view that single fibres are reliable sources of purified myosin isoforms for IVMA.