-transparent.png){kind=logo}
The interaction of streptokinase with diethylpyrocarbonate resulting in partial inactivation of the protein was studied. Eight histidine residues are blocked per streptokinase molecule by this reagent. Ethoxyformylation of streptokinase histidyls is characterized by a rate constant corresponding to modification of free L-histidine. No reactivation of streptokinase was achieved by treatment of the modified protein with hydroxylamine. The CD spectroscopy data suggest that the residues modified by diethylpyrocarbonate are of no consequence for the stabilization of the protein secondary structure. The specificity of modification of streptokinase histidine residues by diethylpyrocarbonate is discussed. Based on the gel chromatography data, it was assumed that partial inactivation of streptokinase depends on the formation of protein oligomers with a decreased activatory function.
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
November 1984,
Journal of biochemistry,
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
February 1977,
Biokhimiia (Moscow, Russia),
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
March 1993,
Biokhimiia (Moscow, Russia),
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
September 1974,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
November 1976,
Biokhimiia (Moscow, Russia),
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
October 1993,
Biokhimiia (Moscow, Russia),
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
August 1976,
Journal of biochemistry,
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
May 1974,
European journal of biochemistry,
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
December 1976,
FEBS letters,
V N Nikandrov, and
O A Kaziuchits, and
G S Iankovskaia
January 1977,
Methods in enzymology,
