Worm Breeder's Gazette 1(2): 23
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
Purified native myosin (1) from the paralyzed mutant E675 has two heavy chains which can be resolved by sodium dodecyl sulfate polyacrylamide gel electrophoresis (2). The ratio of the two chains remains constant within 10% during purification. We have fractionated native myosin from this mutant by hydroxyapatite chromatography and have demonstrated the existence of homologous myosin molecules composed only of one kind of heavy chain. Comparison on 8M urea- sodium dodecyl sulfate polyacrylamide gels of cyanogen bromide cleaved fragments (3) from pooled fractions enriched for either homologous myosin reveals multiple differences in primary structure. Similar peptide differences have been obtained with analogous chromatographic fractions from N2 myosin. These results suggest that at least two structural genes code for myosin heavy chains. Material from the center of the E675 chromatogram contains approximately equal quantities of both heavy chains and rebands true on hydroxyapatite, indicating the existence of a heterologous form of myosin. If this represents a heterologous myosin, it would demonstrate that the two heavy chain types arise from the body wall muscle cells. We are currently investigating this possibility.