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JBC, Vol. 250, Issue 15, 5906-5914, Aug, 1975
J. H. Collins and M. Elzinga
Three of the 17 peptides produced when actin is treated with cyanogen
bromide are sparingly soluble at pH values near neutrality. They were
separated from more soluble peptides at pH 6.0 on a column of Sephadex
G-10. The soluble peptides were excluded from the gel and emerged at the
void volume, while the insoluble peptides were "washed off" by the formic
acid in which the sample was applied. The three insoluble peptides were
sequenced as a group by studying peptides generated by tryptic and
chymotryptic digestion of the mixture, and peptic digestion of the
partially resolved peptides. The three peptides are: CB-15 (residues 133 to
176), CB-16 (residues 325 to 354), and CB-17 (residues 191 to 227).
The primary structure of actin from rabbit skeletal muscle. Three cyanogen bromide peptides that are insoluble at neutral pH
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