What question did this study set out to answer?

Establish a reliable and accurate chemical procedure to quantitatively measure tryptophan concentrations in intact proteins and protein hydrolysates.

October 15, 1949Analytical Chemistry

Chemical Determination of Tryptophan in Proteins

View Full Paper

Ask AI

Bookmark

Authors

JSJoseph R. SpiesUnited States Department of Agriculture DCDorris C. ChambersProvidence Hospital

Discussion

Member takes

Implication

Methodological study demonstrates a chemical assay for quantifying tryptophan in intact and hydrolyzed proteins, indicating reliable amino acid profiling.

Key Points

Establish a reliable and accurate chemical procedure to quantitatively measure tryptophan concentrations in intact proteins and protein hydrolysates.
Developed a direct colorimetric analytical procedure targeting the indole ring of tryptophan within intact protein structures.
Optimized reaction conditions to prevent oxidative and acidic degradation of tryptophan during chemical measurement.
Achieved consistent and reproducible recovery of tryptophan across varied protein substrates without requiring destructive acid hydrolysis.
Overcame traditional interference from secondary amino acids and reagents, establishing a standardized spectrophotometric determination protocol.

Cite This Study

Spies et al. (1949) studied this question.

synapsesocial.com/papers/6a1a15c73f3ec013f0df7641 https://doi.org/10.1021/ac60034a033

View Full Paper

Ask AI

Bookmark

Implication

Methodological study demonstrates a chemical assay for quantifying tryptophan in intact and hydrolyzed proteins, indicating reliable amino acid profiling.

Chemical Determination of Tryptophan in Proteins

Discussion

Member takes

Implication

Key Points

Cite This Study

Chemical Determination of Tryptophan in Proteins

Discussion

Member takes

Implication

Key Points

Cite This Study

Also Consider

Also Consider