-transparent.png){kind=logo}
The effect of modification of basic pancreatic trypsin inhibitor (BPTI) by derivatives of fatty acids (oleic, stearic) on the inhibition of bovine trypsin and human leukocyte elastase (HLE) was studied. Kinetic constants of interaction with trypsin and inhibition constants of both enzymes were determined. Hydrophobization of BPTI had virtually no effect on its high affinity for trypsin. The coupling of cis-unsaturated oleoyl radicals to the inhibitor molecule significantly increased the efficiency of HLE inhibition, whereas the coupling of saturated stearoyl radicals completely canceled the anti-elastase activity and in some cases promoted the substrate hydrolysis.
Related Publications
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
September 1978,
Archives of biochemistry and biophysics,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
July 1996,
Biochemistry,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
June 1996,
FEBS letters,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
January 1991,
Journal of enzyme inhibition,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
May 1990,
Biological chemistry Hoppe-Seyler,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
June 1997,
Journal of leukocyte biology,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
December 1984,
Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
June 2003,
Current protein & peptide science,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
June 1987,
Biochemistry,
E V Malykh, and
O P Tyurina, and
N G Balabushevitch, and
N I Larionova
September 1986,
Journal of molecular biology,
