The primary structure of the myosin head
The sequence of the NH2-terminal 808 amino acid residues of chicken pectoralis muscle myosin head was determined. Three characteristic 20-, 23-, and 50-kDa fragments were isolated from a digest of myosin subfragment 1 (S1) by gel filtration on a Sephadex G-100 column in the presence of 5 M guanidine...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 84; no. 2; pp. 416 - 420 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
National Academy of Sciences of the United States of America
01.01.1987
National Acad Sciences |
Subjects | |
Online Access | Get full text |
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Summary: | The sequence of the NH2-terminal 808 amino acid residues of chicken pectoralis muscle myosin head was determined. Three characteristic 20-, 23-, and 50-kDa fragments were isolated from a digest of myosin subfragment 1 (S1) by gel filtration on a Sephadex G-100 column in the presence of 5 M guanidine hydrochloride, followed by anion-exchange chromatography on a QAE-Sephadex A-50 column in the presence of 8 M urea. The fragments were sequenced completely by conventional methods. Peptides overlapping the 23- and 50-kDa fragments and also overlapping the 50- and 20-kDa fragments were obtained by cleaving S1 with cyanogen bromide. Comparison of the 23-kDa and 50-kDa sequences with that of the overlapping peptide indicated that no additional amino acid exists between the 23- and 50-kDa fragments and that 5 amino acids exist between the 50- and 20-kDa fragments of S1. Methylated amino acid residues were found at four positions: ε -N-monomethyllysine at position 35, ε -N-trimethyllysine residues at 130 and 550, and 3-N-methylhistidine at 754. |
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Bibliography: | 8720998 L50 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.84.2.416 |