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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

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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.

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Implication

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

Cite This Study

Spies et al. (1949) studied this question.

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

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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

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Discussion

Implication

Cite This Study

Chemical Determination of Tryptophan in Proteins

Key Points

Discussion

Implication

Cite This Study

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