Abstract
The addition of 3% ( w v) phenol to 6 M HCl largely prevented the destruction of tryptophan during rapid hydrolysis of peptides and proteins at 166°C for 25 min or at 145°C for 4 h. This hydrolysis procedure was advantageous for amino acid microanalysis using conventional high-performance liquid chromatography with a precolumn derivatization technique. The recovery of tryptophan from proteins was at least 80%. The addition of phenol also improved the recovery of methionine and carboxymethylcysteine. The amount of tryptophan in proteins electroblotted onto a polyvinylidene difluoride membrane was determined by this method.
| Original language | English |
|---|---|
| Pages (from-to) | 223-230 |
| Number of pages | 8 |
| Journal | Analytical Biochemistry |
| Volume | 189 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1990 Sep |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Muramoto, K., & Kamiya, H. (1990). Recovery of tryptophan in peptides and proteins by high-temperature and short-term acid hydrolysis in the presence of phenol. Analytical Biochemistry, 189(2), 223-230. https://doi.org/10.1016/0003-2697(90)90112-M