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JBC, Vol. 252, Issue 7, 2218-2225, Apr, 1977

Automated sequencing of insoluble peptides using detergent. Bacteriophage fl coat protein

G. S. Bailey, D. Gillett, D. F. Hill and G. B. Petersen

Peptides which are highly nonpolar and insoluble under moderate conditions of pH and ionic strength cannot be subjected to automated sequence analysis. We report a method for solubilization of one such peptide, bacteriophage fl coat protein, by chemical modification in the presence of sodium dodecyl sulfate. Following this treatment the 50-residue peptide was degraded stepwise in an automated sequenator using a single cleavage Quadrol program with high repetitive yield through residue 47. We also report a modified program using detergent incorporated into dimethylallylamine buffer which permitted sequencing with high repetitive yields for at least the first 18 residues of the unmodified and otherwise highly insoluble coat protein. The presence of detergent caused no observable difficulties in detection of residues by gas chromatography, thin layer chromatography, or amino acid analysis.
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