Results 91 to 100 of about 5,000 (140)
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Hydrolysis of enkephalin by cultured human endothelial cells and by purified peptidyl dipeptidase
Biochemical Pharmacology, 1978Abstract : The experiments indicate that rapid inactivation of enkephalins may be due to at least two different enzymes present in tissues. A peptidyl dipeptidase which is a component of plasma membrane of various cells may degrade enkephalins by liberating a C-terminal dipeptide and an aminopeptidase in endothelial cells may cleave peptides, that they
A R Johnson, Alice R Johnson, E G Erdos
exaly +3 more sources
Determination of peptidyl dipeptidase activity in 24 bacterial species
Canadian Journal of Microbiology, 1990Of 24 bacterial species examined for lisinopril refractive peptidyl dipeptidase activity, only 8 contained activity. Activity in Pseudomonas maltophilia was more than fourfold higher than that of any other species. Pseudomonas maltophilia may be unique among bacteria in possessing high peptidyl dipeptidase activity that is both EDTA inhibitable and ...
Joseph J Lanzillo +2 more
exaly +3 more sources
Amino acid residues essential for catalysis by peptidyl dipeptidase-4 from pseudomonas maltophilia
Biochemical and Biophysical Research Communications, 1989To assess residues essential for catalysis by prokaryotic peptidyl dipeptidase-4, the enzyme was subjected to chemical modification by a series of reagents. Treatment with either tetranitromethane or N-acetylimidazole abolished catalytic activity. Hydroxylamine reversed inactivation by acetylimidazole only.
Joseph J Lanzillo +2 more
exaly +3 more sources
Biochemical and Biophysical Research Communications, 1989
Peptidyl dipeptidase-4 from Pseudomonas maltophilia was modified with the arginine reagents p-hydroxyphenylglyoxal and 2,3-butanedione. The enzyme was inactivated in a pseudo-first-order manner by p-hydroxyphenylglyoxal with a half-time of 72 min. Inactivation by 2,3-butanedione was biphasic with a rapid phase followed by a slower inactivation to less ...
Joseph J Lanzillo +2 more
exaly +3 more sources
Peptidyl dipeptidase-4 from Pseudomonas maltophilia was modified with the arginine reagents p-hydroxyphenylglyoxal and 2,3-butanedione. The enzyme was inactivated in a pseudo-first-order manner by p-hydroxyphenylglyoxal with a half-time of 72 min. Inactivation by 2,3-butanedione was biphasic with a rapid phase followed by a slower inactivation to less ...
Joseph J Lanzillo +2 more
exaly +3 more sources
Life Sciences, 1981
Abstract Peptidyl dipeptidase activity distinct from the angiotensin converting enzyme (EC 3.4.15.1) was isolated from membrane fractions of rabbit kidney and lung. The enzyme cleaved Leu-enkephalin at the Gly-Phe bond, releasing Tyr-Gly-Gly and Phe-Leu, and also acted on bradykinin releasing the terminal dipeptide Phe-Arg.
N Marks, M J Berg, M J Berg
exaly +3 more sources
Abstract Peptidyl dipeptidase activity distinct from the angiotensin converting enzyme (EC 3.4.15.1) was isolated from membrane fractions of rabbit kidney and lung. The enzyme cleaved Leu-enkephalin at the Gly-Phe bond, releasing Tyr-Gly-Gly and Phe-Leu, and also acted on bradykinin releasing the terminal dipeptide Phe-Arg.
N Marks, M J Berg, M J Berg
exaly +3 more sources
EFFECT OF PEPTIDYL‐DIPEPTIDASE INHIBITORS IN EXPERIMENTAL CONVULSIONS IN MICE
Fundamental & Clinical Pharmacology, 1987Summary— The anticonvulsant effect of compounds that inhibit peptidyl‐dipeptidase (PDP) on bicuculline (BIC)‐ and strychnine (STRYC)‐induced seizures was assessed after intracerebroventricular (ICV) or intraperitoneal (IP) administration in Swiss albino mice.
F J, Miñano +3 more
openaire +2 more sources

