Two smooth muscle myosin heavy chains differ in their light meromyosin fragment
- 1 May 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (10) , 3807-3811
- https://doi.org/10.1021/bi00410a043
Abstract
Smooth muscle myosin heavy chains [SM1, approximately 205 kilodaltons (kDa), and SM2, approximately 200 kDa] were separated on sodium dodecyl sulfate (SDS)-polyacrylamide gels. Peptide maps of the two heavy chains showed unique patterns. Limited proteolytic cleavage of purified swine stomach myosin was performed by using a variety of proteases to produce the major myosin fragments which were resolved on SDS gels. A single band was obtained for heavy meromyosin in the soluble fraction following chymotrypsin digestion. However, a variable number of bands were observed for light meromyosin fragments in the insoluble fraction after chymotrypsin digestion. Peptide mapping indicated that the two bands observed after short digestion times with chymotrypsin had relatively mobility and solubility properties consistent with approximately 100- and 95-kDa light meromyosin (LMM) fragments. These results indicate that the region of difference between SM1 and SM2 lies in the LMM fragment.This publication has 21 references indexed in Scilit:
- Protein structural domains in the Caenorhabditis elegans unc-54 myosin heavy chain gene are not separated by introns.Proceedings of the National Academy of Sciences, 1983
- Improved methodology for analysis and quantitation of proteins on one-dimensional silver-stained slab gelsAnalytical Biochemistry, 1983
- Binding of gizzard smooth muscle myosin subfragment-1 to actin in the presence and absence of adenosine 5'-triphosphateBiochemistry, 1983
- A dot-immunobinding assay for monoclonal and other antibodiesAnalytical Biochemistry, 1982
- Myosin Phosphorylation and the Cross-Bridge Cycle in Arterial Smooth MuscleScience, 1981
- Tight binding of arterial myosin to skeletal F-actin.Journal of Biological Chemistry, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Electrophoretic analysis of multiple forms of rat cardiac myosin: Effects of hypophysectomy and thyroxine replacementJournal of Molecular and Cellular Cardiology, 1978
- Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.Journal of Biological Chemistry, 1977
- Electrophoretic analysis of multiple forms of myosin in fast-twitch and slow-twitch muscles of the chickBiochemical Journal, 1976