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Ionization behavior of proteins. I. Spectral titration of the tyrosyl groups of chymotrypsinogen and nitrated-chymotrypsinogen

✍ Scribed by Charles J. Martin; Mario A. Marini

Book ID: 101718814
Publisher: Wiley (John Wiley & Sons)
Year: 1982
Tongue: English
Weight: 492 KB
Volume: 21
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360210814

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✦ Synopsis

The ionization constants of the tyrosyl groups of chymotrypsinogen and of nitrated-chymotrypsinogen (two tyrosyl residues nitrated) have been determined by difference spectrophotometry. In chymotrypsinogen. two of the four tyrosyl groups ionize without any time dependence. Above pH greater than ca. 12.5, time-dependent spectral changes are seen for 0.7 group equivalent. The data can be fitted to the values of pK', 9.75 f 0.07, pKi 11.55 f 0.05, pK' 13.30 f 0.05. In nitrated-chymotrypsinogen, the two nitrated tyrosyl residues have pK; 6.44 and pK; 8.30. For both proteins, these pK' values are in agreement with those evaluated from potentiometric titration and calorimetric data using computer-assisted curve-fitting analysis.

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