Jun 1, 1976

Complete tyrosine assignments in the high-field 1H nuclear magnetic resonance spectrum of bovine pancreatic trypsin inhibitor selectively reduced and carboxamidomethylated at cystine 14-38

Biochemistry
G H SnyderB D Sykes

Abstract

The low-field portions of the 250-MHz 1H nuclear magnetic resonance spectra of native and chemically modified basic pancreatic trypsin inhibitor have been studied as a function of pH over the range pH 5-13. In derivatives selectively reduced and carboxamidomethylated at cystine 14-38, resonances associated with 15 of the 16 protons of the aromatic rings of the four tyrosines of the inhibitor have been located and assigned to specific tyrosyl residues. Titrations of pH yielded pK's for tyrosines 10, 21, 23, and 35 in the modified inhibitor of 9.9, 10.6, 11.6, and 11.0, respectively. Resonances associated with the three nitrotyrosine 10 protons of the mononitrated derivative and the six nitrotyrosine 10 and 21 protons of the dinitrated derivative have been similarly located, assigned, and titrated, yielding pK's for nitrotyrosines 10 and 21 of 6.5 and 6.4, respectively. Previously reported results for derivatives with cystine 14-38 intact have been revised on the basis of new data. Comparison of these revised results with the new data for derivatives with modified cystine 14-38 reveals no changes in pK's for any tyrosine or nitrotyrosing ring and no changes in chemical shift for resonances of nitrotyrosine 21 or tyrosines 21 and ...Continue Reading

Mentioned in this Paper

In Vivo NMR Spectroscopy
Carmol
Plasma Protein Binding Capacity
Zymofren
Protein Conformation
Guanidines
Bos indicus
Copper Cystinate
Tyrosine
Hydrogen-Ion Concentration

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