Summary
Acid hydrolysis of trypsin and chymotrypsin inhibited by DIP yields seryl-phosphate within a sequence representing one part of the ‘active center’. Now it is demonstrated by UV-spectrophotometry that DIP is bound primarily to tryptophane and remains there after peptic degradation. A tetrapeptide containing both tryptophane and phosphate was isolated and analyzed.
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References
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Simon, K. Tryptophan im aktiven Zentrum von Trypsin und Chymotrypsin. Experientia 18, 150–151 (1962). https://doi.org/10.1007/BF02153870
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DOI: https://doi.org/10.1007/BF02153870