Phosphorylation site sequence of smooth muscle myosin light chain (Mr = 20 000)
Open Access
- 12 March 1984
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 168 (1) , 108-112
- https://doi.org/10.1016/0014-5793(84)80216-1
Abstract
The amino terminal sequence of the myosin light chain (M r = 20 000) isolated from chicken gizzards was found to be acetyl‐Ser‐Ser‐Lys‐Arg‐Ala‐Lys‐Ala‐Lys‐Thr‐Thr‐Lys‐Lys‐Arg‐Pro‐Gln‐Arg‐Ala‐Thr‐Ser(P)‐Asn‐Val‐Phe. This sequence assignment differs from that reported by Maita et al. [(1981) European J. Biochem. 117, 417] in the order of the tryptic peptides. The revised amino acid sequence exhibits greater homology with the phosphorylation site sequences of the regulatory light chains from cardiac and skeletal muscle. Moreover it is now apparent why synthetic peptides corresponding to the previously reported sequence were very poor substrates for the myosin light chain kinase.Keywords
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