Studies on the proteins of fish skeletal muscle. 3. Cod myosin and cod actin
- 1 November 1954
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 58 (3), 360-367
- https://doi.org/10.1042/bj0580360
Abstract
By modifying the extraction methods, proteins could be extracted from cod muscle resembling rabbit myosin and actin. Cod myosin resembles rabbit myosin in appearance, solubility behavior to adenosine triphosphate (ATP) and F-actin, electro-phoretic behavior, and instrinsic viscosity, but the sedimentation constant and diffusion constant were much closer to the values for actomyosin. These give the same axial ratio of 50 but a molecular weight at least double that of rabbit myosin. Cod F-actin is more easily extracted than rabbit due to the lack of stroma. It closely resembles rabbit actin in physical and chemical properties and gives a molecular weight of 160,000 from osmotic pressure, although ultra-centrifuge data indicate the molecular dimensions are uncertain. In 0.6 [image]- KI cod G-actin exists as a dimer.Keywords
This publication has 18 references indexed in Scilit:
- The interaction of myosin with adenosine triphosphateArchives of Biochemistry and Biophysics, 1953
- The molecular dimensions and the monomer-dimer transformation of actinBiochimica et Biophysica Acta, 1953
- Myosin preparations from the rabbit, rat and mouseArchives of Biochemistry and Biophysics, 1952
- THE MOLECULAR TRANSFORMATIONS OF ACTIN .1. GLOBULAR ACTIN1952
- Further investigations on fish tropomyosin and fish nucleotropomyosinBiochemical Journal, 1951
- REVERSIBLE POLYMERIZATION AND ULTRACENTRIFUGAL PURIFICATION OF ACTINJournal of Biological Chemistry, 1951
- Fish tropomyosin and fish nucleotropomyosinBiochemical Journal, 1951
- Sur les protéines extractibles du muscle strié après traitement de la pulpe par quelques solvants organiquesCellular and Molecular Life Sciences, 1950
- Contribution a l'étude de la transformation G-actine - F-actineBiochimica et Biophysica Acta, 1950
- The analysis of the osmotic pressures of the serum proteins, and the molecular weights of albumins and globulinsBiochemical Journal, 1930