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Studies on the Subunit Structure of Myosin
Open accessAbstract
Abstract The low molecular weight protein associated with rabbit skeletal myosin has been estimated by gel filtration studies in 5 m guanidine hydrochloride and was found to constitute 9 ± 2% of the myosin mass. We have found that 40 to 50% of the low molecular weight protein can be removed from myosin without any apparent changes in the adenosine-triphosphatase activity. Attempts to remove a larger fraction of low molecular weight protein resulted in a concomitant loss of enzymatic activity. The molecular weight of the major myosin subunit freed of low molecular weight protein has been redetermined in 5 m guanidine hydrochloride and was found to be 194,000 g per mole. The significance of its presence in assessing the molecular weight of the major subunit at low speed and high speed sedimentation equilibrium has been investigated.
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Citations
Cited by
An electrophoretic study of the low-molecular-weight components of myosin
Perrie, W. T., & Perry, S. V. (1970) · Biochemical Journal · doi:10.1042/bj1190031 · Cited by 706
Weeds, A. G., & Pope, B. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80119-8 · Cited by 630
Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor
Mosher, D. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41110-1 · Cited by 566
Functionality of muscle proteins in gelation mechanisms of structured meat products
Asghar, A., Samejima, K., Yasui, T., & Henrickson, R. L. (1985) · C R C Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398509527408 · Cited by 293
Hoh, J. F. Y., McGrath, P. A., & White, R. I. (1976) · Biochemical Journal · doi:10.1042/bj1570087 · Cited by 280
Metadata
- Authors
- Gazith, J., Himmelfarb, S., & Harrington, W. F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1970-01
- Volume
- 245
- Issue
- 1
- Pages
- 15-22
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1507842415
- Cited by
- 199
- References
- 0
- FWCI
- 22.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
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