Pearson R B, Jakes R, John M, Kendrick-Jones J, Kemp B E
FEBS Lett. 1984 Mar 12;168(1):108-12. doi: 10.1016/0014-5793(84)80216-1.
The amino terminal sequence of the myosin light chain (Mr = 20 000) isolated from chicken gizzards was found to be (sequence in text). 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.
从鸡砂囊中分离出的肌球蛋白轻链(分子量 = 20000)的氨基末端序列被发现为(文中序列)。该序列分配在胰蛋白酶肽的顺序上与Maita等人[(1981年)《欧洲生物化学杂志》117卷,417页]报道的不同。修订后的氨基酸序列与心肌和骨骼肌调节轻链的磷酸化位点序列具有更高的同源性。此外,现在很明显为什么对应于先前报道序列的合成肽是肌球蛋白轻链激酶的非常差的底物。