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JBC, Vol. 251, Issue 7, 1936-1940, Apr, 1976
R. J. Simpson, M. R. Neuberger and T. Y. Liu
An analytical procedure which affords the precise amino acid composition of
a protein or a peptide from a single hydrolysate is described. This method
utilizes 4 N methanesulfonic acid containing 0.2% 3-(2-aminoethyl)indole,
rather then 6N HCl as a catalyst for hydrolysis. The hydrolysis is carried
out in vacuo (20 mu) at 115 degrees for 22 to 72 hours. Half-cystine is
determined as S-sulfocysteine by treating the hydrolysate with
dithiothreitol followed by an excess of tetrathionate. The values of all
amino acids, including tryptophan and half-cystine, were close to the
expected theoretical values for the proteins examined. The method has the
advantage that the neutralized hydrolysate can be applied directly to an
ion exchange column. Further, the method is capable of distinguishing
between free sulfhydryl groups as S-carbosymethylcysteine and disulfides as
S-sulfocysteine. A limitation of the procedure is that tryptophan remains
sensitive to the presence of carbohydrate in the sample.
Complete amino acid analysis of proteins from a single hydrolysate
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