Uniform myosin isoforms in the flight muscles of little brown bats,Myotis lucifugus

✍ Scribed by Hermanson, John W. ;LaFramboise, William A. ;Daood, Monica J.

• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: English
• Weight: 843 KB
• Volume: 259
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/jez.1402590205

✦ Synopsis

Abstract

The present study used muscle histochemistry and polyacrylamide gel electrophoresis of native myosin and myosin heavy chains to establish a correlation, if any, between chiropteran histochemical fiber types and myosin isoform composition. Histochemical analysis of the primary flight muscle, the pectoralis profundus, documented the presence of a single histochemical fiber type, here termed Type II. Electrophoresis of native myosin isolated from pectoralis muscle yielded a single isoform that comigrated with the FM‐3 isoform of rat diaphragm. Heavy chain analysis of the Myotis pectoralis demonstrated a single heavy chain with comparable electrophoretic mobility to rat IIa myosin heavy chain. These data demonstrate unique histochemical and biochemicla homogeneity in the myosin composition of the pectoralis muscle of Myotis lucifugus. Thus this muscle is extremely specialized for flight at histochemical, morphologic, and molecular levels. These data contrast with the mixed myosin and histochemical fiber types found in other mammals, as well as in other muscles of Myotis lucifugus.