Preparation of the alkali and P light chains of chicken gizzard myosin. Amino acid sequence of the alkali light chain
- 1 April 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 211 (1) , 267-272
- https://doi.org/10.1042/bj2110267
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.This publication has 16 references indexed in Scilit:
- The Amino Acid Sequence of the δ Subunit (Calmodulin) of Rabbit Skeletal Muscle Phosphorylase KinaseEuropean Journal of Biochemistry, 1981
- Structure And Evolution Of Calcium-Modulated ProteinCritical Reviews in Biochemistry, 1980
- Involvement of 17K Dalton Light Chain of Smooth Muscle Myosin in Substrate-Induced Conformational ChangeThe Journal of Biochemistry, 1980
- Effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation.Proceedings of the National Academy of Sciences, 1977
- Calcium binding regions of myosin ‘Regulatory’ light chainsFEBS Letters, 1976
- The effect of phosphorylation of gizzard myosin on actin activationBiochemical and Biophysical Research Communications, 1976
- Solid‐phase edman degradation: Attachment of carboxyl‐terminal homoserine peptides to an insoluble resinFEBS Letters, 1973
- The subunit structure of gizzard myosinPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1973
- The regulatory proteins of the myofibril. Separation and biological activity of the components of inhibitory-factor preparationsBiochemical Journal, 1972
- An electrophoretic study of the low-molecular-weight components of myosinBiochemical Journal, 1970