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Journal of Experimental Biology, Vol 183, Issue 1 185-202, Copyright © 1993 by Company of Biologists
JOURNAL ARTICLES |
D. M. Neil, W. S. Fowler and G. Tobasnick
The myofibrillar proteins in fibres from the abdominal flexor muscles of the Norway lobster, Nephrops norvegicus, have been identified using SDS-PAGE gel electrophoresis. Several contractile and regulatory proteins are expressed as multiple isoforms in single fibres and, according to these, one fast fibre phenotype (F) can be identified in the deep flexor muscles and two slow fibre phenotypes (S1 and S2) can be distinguished in the superficial flexor muscles. The two slow fibre phenotypes are distributed non-uniformly across the superficial flexor muscle, and in the lateral bundle there is a heterogeneous mixture of both S1 and S2 fibres. Using histochemical procedures applied to intact or freeze-dried fibres in conjunction with measurements of fibre sarcomere length and gel electrophoresis, an exact correspondence can be demonstrated between the morphological properties, enzymatic content and myofibrillar protein composition of individual fibres from the deep and superficial flexor muscles. In the superficial flexor muscle, fibres of the S1 phenotype have a mean sarcomere length of <8 micrometre, a low oxidative capacity and an acid-labile isoform of myosin ATPase, while fibres of the S2 phenotypes have a longer sarcomere length (mean >9 micrometre), a higher oxidative capacity and an acid-stable isoform of myosin ATPase. These results are discussed in terms of the relationships between the different muscle fibre properties and the usefulness of procedures applied to single fibres for determining them.
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