[Determination of angiotensin-converting enzyme activity using dansyl-Phe-Ala-Arg as the substrate].

Modificated method for the determination of the angiotensin converting enzyme (EC 3.4.15.

[Effect of sodium hydroxybutyrate on carboxypeptidase H activity and on angiotensin-converting enzyme in different regions of the rat brain].

It is revealed, that analogue of the gamma-aminobutyric acid--sodium hydroxybutyrate causes decrease of activities carboxypeptidase H and angiotensin converting enzyme in pituitary gland, hypothalamus and striatum. The most expressed changes of enzyme activities were observed in pituitary gland and hypothalamus. The activity of carboxypeptidase H changes more essentially, than one of angiotensin converting enzyme.

[Basic carboxypeptidase activity in rats of both sexes].

The activity of carboxypeptidase (CP) H, the enzyme taking part in neuropeptide formation, and activity of recently described phenylmethylsulfonyl fluoride (PMSF)--inhibiting CP in males and females of white mongrel rats were studied. Minor differences between the CPH activities in brain regions were found in hippocampus. PMSF-inhibited activity of carboxypeptidase was significantly higher in females than in males in pituitary gland, adrenal gland, olfactory bulbus, optic and auditory bills, cerebellum, hippocampus, striatum, cerebral hemispheres and spleen.

[Tissue and regional distribution of activity of phenylmethylsulfonyl fluoride inhibited carboxypeptidase and other carboxypeptidases in rats].

Phenylmethylsulfonyl fluoride (PMSF)-inhibited carboxypeptidase (CP) is recently described exopeptidase, that cleaved arginine residues from C-terminal of enkephalin synthetic analogs. The highest enzyme activity was found in the adrenal gland and 40% lower one was revealed in the pituitary gland. A 2.