An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscles. Purification from bovine aorta
- 15 June 1987
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 244 (3) , 705-709
- https://doi.org/10.1042/bj2440705
Abstract
Using a rabbit polyclonal-antibody preparation directed against the chicken gizzard protein, we demonstrated by immunoblotting the presence of the 22 kDa protein (SM22) in a variety of chicken smooth-muscle-containing organs, including uterus, intestine, gizzard, oesophagus and aorta. Protein SM22 was present in only trace amounts in brain, liver and heart, and could not be detected in chicken breast muscle. The antibody preparation did not cross-react with extracts of bovine aorta. However, the presence of SM22 as a major component in bovine aorta and pig carotid was demonstrated by its co-migration with the purified chicken gizzard protein on one- and two-dimensional polyacrylamide electrophoretic gels. Its molar abundance relative to actin was estimated to be 0.9:6.0 and 1.4:6.0 for bovine aorta and pig carotid respectively. Like the chicken gizzard protein, it separates on pH-gradient electrophoresis into at least three variants, .alpha., .beta. and .gamma., with similar apparent Mr. Purification of the aorta SM22 showed it to have a similar amino acid composition to the chicken gizzard protein. We conclude that SM22 is widely distributed and an abundant and unique protein component of smooth-muscle tissues of birds and mammals.This publication has 17 references indexed in Scilit:
- The thin filaments of smooth musclesJournal of Muscle Research and Cell Motility, 1985
- Phosphorylation of myosin light chain kinase from vascular smooth muscle by cAMP- and cGMP-dependent protein kinasesJournal of Molecular and Cellular Cardiology, 1985
- Bovine aorta actin. Development of an improved purification procedure and comparison of polymerization properties with actins from other types of muscleBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Application of the nitrocellulose transfer technique and alkaline phosphatase conjugated anti-immunoglobulin for determination of the specificity of monoclonal antibodies to protein mixturesJournal of Immunological Methods, 1982
- The Croonian Lecture, 1979: Regulation of muscle contractionProceedings of the Royal Society of London. B. Biological Sciences, 1980
- [28] Enzyme immunoassay ELISA and EMITPublished by Elsevier ,1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Differences in cellular contractile protein contents among porcine smooth muscles: evidence for variation in the contractile system.The Journal of general physiology, 1978
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970