Abstract
DURING studies on the primary structure of certain regions of rabbit skeletal muscle myosin, we have found that this protein contains an average of 5.9 moles of the unusual amino-acid, ε-N-methyl lysine, per 500,000 g of myosin. In analysing myosin digestion products we observed a trailing edge after the lysine peak which could be resolved from lysine and histidine only by altering the elution programme and extending the basic column. The conditions which provided a satisfactory resolution of this peak, as well as of 3-methyl histidine, which has previously been found in actin and myosin1,2, are as follows.
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HUSZAR, G., ELZINGA, M. ε-N-Methyl Lysine in Myosin. Nature 223, 834–835 (1969). https://doi.org/10.1038/223834a0
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DOI: https://doi.org/10.1038/223834a0
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