-transparent.png){kind=logo}
Mass spectrometry has been used to provide insights into the mechanism of inhibition of cysteine proteases by a hydroxylamine derivative, CBZ-Phe-Gly-NH-O-CO-(2,4,6-Me3)Ph. An oxidized form of papain resulting from the incubation of the enzyme with the peptidyl hydroxamate in the absence of a reducing agent has been identified as a sulfinic acid. The presence of a covalent enzyme-inhibitor complex of molecular mass consistent with a sulfenamide adduct of papain could also be detected by this method. Implications on the mechanism of inactivation of cysteine proteases by peptidyl hydroxamates are discussed.
Related Publications
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
November 1989,
The Biochemical journal,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
June 1995,
Biochemistry,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
November 1993,
Journal of biochemistry,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
September 1988,
Biochemical and biophysical research communications,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
March 2011,
Proteins,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
January 1988,
Journal of enzyme inhibition,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
January 1972,
Biochemistry,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
October 1993,
Biochimica et biophysica acta,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
September 1957,
Biochimica et biophysica acta,
R Ménard, and
R Feng, and
A C Storer, and
V J Robinson, and
R A Smith, and
A Krantz
July 1967,
Biochimica et biophysica acta,
