Abstract
β-Actinin is an actin-pointed end capping protein in skeletal muscle. Casella et al. have reported that a protein isolated from muscle acetone powder by procedures similar to those used for βactinin purification caps the barbed end of an actin filament (J. Biol. Chem. 261, 10915-10921 (1986)). We have confirmed the above results. However, it turned out that the two proteins were identical as to subunit sizes, peptide maps, and cross-reactivities with anti-β-actinin IgG. The binding of the two proteins to opposite ends of an actin filament remains unexplained.
| Original language | English |
|---|---|
| Pages (from-to) | 1481-1483 |
| Number of pages | 3 |
| Journal | Journal of Biochemistry |
| Volume | 101 |
| Issue number | 6 |
| Publication status | Published - 1987 |
ASJC Scopus subject areas
- Statistics, Probability and Uncertainty
- Applied Mathematics
- Physiology (medical)
- Radiology Nuclear Medicine and imaging
- Molecular Biology
- Biochemistry
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Oosawa, M., Shimaoka, S., Funatsu, T., Ishiwata, S., & Maruyama, K. (1987). βactinin is not distinguishable from an actin barbed-end capping protein in chicken breast muscle. Journal of Biochemistry, 101(6), 1481-1483.