Abstract
1. A simple method is described for the purification of the alkali and P light chains from chicken gizzard myosin. 2. The sequence of the alkali light chain has been unequivocally determined, except for the N-terminal dipeptide, by using the tryptic and CNBr peptides. 3. No evidence was obtained for any specific high-affinity Ca2+-binding sites on the alkali light chain. 4. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50120 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1983) 209, 5.
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- Chacko S., Conti M. A., Adelstein R. S. Effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation. Proc Natl Acad Sci U S A. 1977 Jan;74(1):129–133. doi: 10.1073/pnas.74.1.129. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cole H. A., Grand R. J., Perry S. V. Non-correlation of phosphorylation of the P-light chain and the actin activation of the ATPase of chicken gizzard myosin. Biochem J. 1982 Aug 15;206(2):319–328. doi: 10.1042/bj2060319. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grand R. J., Shenolikar S., Cohen P. The amino acid sequence of the delta subunit (calmodulin) of rabbit skeletal muscle phosphorylase kinase. Eur J Biochem. 1981 Jan;113(2):359–367. doi: 10.1111/j.1432-1033.1981.tb05074.x. [DOI] [PubMed] [Google Scholar]
- Górecka A., Aksoy M. O., Hartshorne D. J. The effect of phosphorylation of gizzard myosin on actin activation. Biochem Biophys Res Commun. 1976 Jul 12;71(1):325–331. doi: 10.1016/0006-291x(76)90286-2. [DOI] [PubMed] [Google Scholar]
- Horn M. J., Laursen R. A. Solid-phase edman degradation: attachment of carboxyl-terminal homoserine peptides to an insoluble resin. FEBS Lett. 1973 Nov 1;36(3):285–288. doi: 10.1016/0014-5793(73)80392-8. [DOI] [PubMed] [Google Scholar]
- Jakes R., Northrop F., Kendrick-Jones J. Calcium binding regions of myosin 'regulatory' light chains. FEBS Lett. 1976 Nov;70(1):229–234. doi: 10.1016/0014-5793(76)80763-6. [DOI] [PubMed] [Google Scholar]
- Kendrick-Jones J. The subunit structure of gizzard myosin. Philos Trans R Soc Lond B Biol Sci. 1973 Mar 15;265(867):183–189. doi: 10.1098/rstb.1973.0021. [DOI] [PubMed] [Google Scholar]
- Kretsinger R. H. Structure and evolution of calcium-modulated proteins. CRC Crit Rev Biochem. 1980;8(2):119–174. doi: 10.3109/10409238009105467. [DOI] [PubMed] [Google Scholar]
- Maita T., Chen J. I., Matsuda G. Amino-acid sequence of the 20 000-molecular-weight light chain of chicken gizzard-muscle myosin. Eur J Biochem. 1981 Jul;117(2):417–424. doi: 10.1111/j.1432-1033.1981.tb06354.x. [DOI] [PubMed] [Google Scholar]
- Matsuda G., Maita T., Kato Y., Chen J. I., Umegane T. Amino acid sequences of the cardiac L-2A, L-2B and gizzard 17 000-Mr light chains of chicken muscle myosin. FEBS Lett. 1981 Dec 7;135(2):232–236. doi: 10.1016/0014-5793(81)80789-2. [DOI] [PubMed] [Google Scholar]
- Mikawa T., Toyo-oka T., Nonomura Y., Ebashi S. Essential factor of gizzard "troponin" fraction. A new type of regulatory protein. J Biochem. 1977 Jan;81(1):273–275. doi: 10.1093/oxfordjournals.jbchem.a131447. [DOI] [PubMed] [Google Scholar]
- Okamoto Y., Sekine T. Involvement of 17K dalton light chain of smooth muscle myosin in substrate-induced conformational change. J Biochem. 1980 Jan;87(1):167–178. doi: 10.1093/oxfordjournals.jbchem.a132722. [DOI] [PubMed] [Google Scholar]
- Perrie W. T., Perry S. V. An electrophoretic study of the low-molecular-weight components of myosin. Biochem J. 1970 Aug;119(1):31–38. doi: 10.1042/bj1190031. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sobieszek A. Ca-linked phosphorylation of a light chain of vertebrate smooth-muscle myosin. Eur J Biochem. 1977 Mar 1;73(2):477–483. doi: 10.1111/j.1432-1033.1977.tb11340.x. [DOI] [PubMed] [Google Scholar]
- Wilkinson J. M. A method for purifying methionine-containing peptides by radioactive labelling. FEBS Lett. 1969 Aug;4(3):170–172. doi: 10.1016/0014-5793(69)80226-7. [DOI] [PubMed] [Google Scholar]
- Wilkinson J. M., Perry S. V., Cole H. A., Trayer I. P. The regulatory proteins of the myofibril. Separation and biological activity of the components of inhibitory-factor preparations. Biochem J. 1972 Mar;127(1):215–228. doi: 10.1042/bj1270215. [DOI] [PMC free article] [PubMed] [Google Scholar]