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SPEEDS OF ACTIN TRANSLOCATION IN VITRO BY MYOSINS EXTRACTED FROM SINGLE RAT MUSCLE FIBRES OF DIFFERENT TYPES

Published online by Cambridge University Press:  04 January 2001

M. CANEPARI ,
R. ROSSI ,
M. A. PELLEGRINO ,
C. REGGIANI  and
R. BOTTINELLI
M. CANEPARI
Affiliation:
Institute of Human Physiology, University of Pavia, via Forlanini 6, 27100 Pavia, Italy
R. ROSSI
Affiliation:
Institute of Human Physiology, University of Pavia, via Forlanini 6, 27100 Pavia, Italy
M. A. PELLEGRINO
Affiliation:
Institute of Human Physiology, University of Pavia, via Forlanini 6, 27100 Pavia, Italy
C. REGGIANI
Affiliation:
Institute of Human Physiology, University of Pavia, via Forlanini 6, 27100 Pavia, Italy
R. BOTTINELLI
Affiliation:
Institute of Human Physiology, University of Pavia, via Forlanini 6, 27100 Pavia, Italy
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Abstract

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.

Type
Rapid Communications
Information
Experimental Physiology , Volume 84 , Issue 4 , July 1999 , pp. 803 - 806
Copyright
© The Physiological Society 1999

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