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- APPEL P., GINSBURG A., SCHACHMAN H. K. Molecular-weight determinations during the approach to sedimentation equilibrium. Arch Biochem Biophys. 1956 Dec;65(2):545–566. doi: 10.1016/0003-9861(56)90213-2. [DOI] [PubMed] [Google Scholar]
- BALDWIN R. L. Boundary spreading in sedimentation-velocity experiments. V. Measurement of the diffusion coefficient of bovine albumin by Fujita's equation. Biochem J. 1957 Mar;65(3):503–512. doi: 10.1042/bj0650503. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BARANY M., BARANY K., GUBA F. Preparation of actin without extraction of myosin. Nature. 1957 Apr 20;179(4564):818–819. doi: 10.1038/179818b0. [DOI] [PubMed] [Google Scholar]
- BLUM J. J., MORALES M. F. The interaction of myosin with adenosine triphosphate. Arch Biochem Biophys. 1953 Mar;43(1):208–230. doi: 10.1016/0003-9861(53)90100-3. [DOI] [PubMed] [Google Scholar]
- BRIGGS D. R., WOLF W. J. Studies on the cold-insoluble fraction of the water-extractable soybean proteins. I. Polymerization of the 11 S component through reactions of sulfhydryl groups to form disulfide bonds. Arch Biochem Biophys. 1957 Nov;72(1):127–144. doi: 10.1016/0003-9861(57)90180-7. [DOI] [PubMed] [Google Scholar]
- CASPARY E. A., KEKWICK R. A. Some physicochemical properties of human fibrinogen. Biochem J. 1957 Sep;67(1):41–48. doi: 10.1042/bj0670041. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CONNELL J. J. Studies on the protein of fish skeletal muscle. 4. Ultracentrifugal analysis of codling extracts. Biochem J. 1958 May;69(1):5–12. doi: 10.1042/bj0690005. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CONNELL J. J. Studies on the proteins of fish skeletal muscle. 3. Cod myosin and cod actin. Biochem J. 1954 Nov;58(3):360–367. doi: 10.1042/bj0580360. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HAMOIR G. Fish proteins. Adv Protein Chem. 1955;10:227–288. doi: 10.1016/s0065-3233(08)60106-0. [DOI] [PubMed] [Google Scholar]
- HAMOIR G., REUTER A. Isolement et propriétés de la myosine de grenouille. Biochim Biophys Acta. 1956 Jul;21(1):24–34. doi: 10.1016/0006-3002(56)90090-7. [DOI] [PubMed] [Google Scholar]
- HOLTZER A. On the spontaneous aggregation of myosin. Arch Biochem Biophys. 1956 Oct;64(2):507–509. doi: 10.1016/0003-9861(56)90294-6. [DOI] [PubMed] [Google Scholar]
- LAKI K., CARROLL W. R. Size of the myosin moleucle. Nature. 1955 Feb 26;175(4452):389–390. doi: 10.1038/175389a0. [DOI] [PubMed] [Google Scholar]
- MILLER G. L., GOLDER R. H., EITELMAN E. S., MILLER E. E. Myosin preparations from the rabbit, rat and mouse. Arch Biochem Biophys. 1952 Nov;41(1):125–137. doi: 10.1016/0003-9861(52)90511-0. [DOI] [PubMed] [Google Scholar]
- MOMMAERTS W. F. H. M. The molecular transformations of actin. I. Globular actin. J Biol Chem. 1952 Sep;198(1):445–457. [PubMed] [Google Scholar]
- MOMMAERTS W. F., RUPP J. C. The scattering of light in myosin solutions. II. A determination of the molecular weight. J Biol Chem. 1957 Jan;224(1):277–293. [PubMed] [Google Scholar]
- NODA L., KUBY S. A., LARDY H. A. Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties. J Biol Chem. 1954 Jul;209(1):203–210. [PubMed] [Google Scholar]
- PARRISH R. G., MOMMAERTS W. F. Studies on myosin. II. Some molecular-kinetic data. J Biol Chem. 1954 Aug;209(2):901–913. [PubMed] [Google Scholar]
- WEBER A. The ultracentrifugal separation of L-myosin and actin in an actomyosin sol under the influence of ATP. Biochim Biophys Acta. 1956 Feb;19(2):345–351. doi: 10.1016/0006-3002(56)90439-5. [DOI] [PubMed] [Google Scholar]