Higuchi, M., Fábián, F., Wandzilak, T., Jr., Mason, D. T. & Wikman-Coffelt, J.

Dissociation of light chains from cardiac myosin.

Eur J Biochem 92, 317-23.

Fábián, F. & Szilágyi, L.

Isolation of the C-terminal peptides of rabbit skeletal myosin.

Acta Biochim Biophys Acad Sci Hung 13, 1-5.

Purified LMM and its tryptic fragments (LF-1, LF-2 and LF-3) were treated with carboxypeptidase-A and the liberated amino acids were identified by thin layer ion-exchange charomatography. In each protein the only detectable amino acid was leucine. From the total tryptic digest of LMM the C-terminal leucine containing peptides were isolated. Two peptides were found with the following amino acid composition: asx1, g1x6, ala1, leu3, and g1n2-3, leu1, respectively. We obtained the same two peptides from the total tryptic digest of LF-3. We conclude that the C-terminal amino acid of the myosin heavy chain is leucine rather than isoleucine as suggested earlier. Heterogeneity of isolated C-terminal peptides might indicate a heterogeneity in the myosin heavy chains.

Bálint, M., Wolf, I., Tarcsafalvi, A., Gergely, J. & Sreter, F. A.

Location of SH-1 and SH-2 in the heavy chain segment of heavy meromyosin.

Arch Biochem Biophys 190, 793-9.