-transparent.png){kind=logo}
The inhibitory effect of catecholamines, their metabolic intermediates and derivatives on the activity of rat brain dipeptidyl aminopeptidase was studied. The enzyme was extracted from a crude mitochondrial fraction containing lysosomes (and also synaptosomes) and purified by three-step column chromatography. The activity of the purified enzyme was inhibited by a low concentration (IC50 2 approximately 5 mM) of dopamine, norepinephrine and epinephrine. Dihydroxyphenylalanine or dihydroxyphenylacetic acid, each having a carboxyl group, showed only a weak inhibitory effect (IC50 greater than 10 mM). These results suggest the possibility that brain dipeptidyl aminopeptidase activity may be regulated by the changing of the concentration of catecholamines in the central nervous system.
K Imai, and
S Saito, and
T Kato
October 1979,
Experientia,
K Imai, and
S Saito, and
T Kato
March 1984,
Experientia,
K Imai, and
S Saito, and
T Kato
February 1983,
Journal of biochemistry,
K Imai, and
S Saito, and
T Kato
December 1980,
Biochemical pharmacology,
K Imai, and
S Saito, and
T Kato
January 1974,
The Journal of biological chemistry,
K Imai, and
S Saito, and
T Kato
November 1983,
Journal of general microbiology,
K Imai, and
S Saito, and
T Kato
July 1994,
The International journal of biochemistry,
K Imai, and
S Saito, and
T Kato
October 1982,
The Journal of biological chemistry,
K Imai, and
S Saito, and
T Kato
January 1987,
Mineral and electrolyte metabolism,
K Imai, and
S Saito, and
T Kato
November 1972,
Activitas nervosa superior,
