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 inProceedings of the National Academy of Sciences - PNAS Vol. 84; no. 2; pp. 416 - 420
Main Authors Maita, T, Hayashida, M, Tanioka, Y, Komine, Y, Matsuda, G
Format Journal Article
LanguageEnglish
Published Washington, DC National Academy of Sciences of the United States of America 01.01.1987
National Acad Sciences
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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.
Bibliography:8720998
L50
ObjectType-Article-1
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content type line 23
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.84.2.416