Results 131 to 140 of about 10,632 (177)
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Peptidyl dipeptidase in rabbit brain microvessels
Biochimica Et Biophysica Acta - Biomembranes, 1978The activity of peptidyl dipeptidase (peptidyldipeptide hydrolase, EC 3.4.15.1), also known as angiotensin-converting enzyme, was studied in small blood vessel preparations isolated from rabbit brain. The vascular preparation contained arterioles and capillaries and was essentially free of extravascular material.
P Brecher, H Gavras, Aram V Chobanian
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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
Ervin G Erdos
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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 ...
Joanne Stevens +2 more
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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.
J J Lanzillo, Barry L Fanburg
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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 ...
J J Lanzillo, Barry L Fanburg
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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 ...
J J Lanzillo, Barry L Fanburg
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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.
M Benuck, Martin J Berg, N Marks
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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.
M Benuck, Martin J Berg, N Marks
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Journal of Neurochemistry, 1990
Abstract: Incubation of various authentic peptides with rat CSF in vitro and analysis of their products by HPLC demonstrated the presence in CSF of a peptidyl dipeptidase [peptidyl dipeptide hydrolase; angiotensin I converting enzyme (ACE); kininase II; EC 3.4.15.1] which sequentially degraded bradykinin (BK) by liberating the carboxy‐terminal ...
Shoichiro Nosaka
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Abstract: Incubation of various authentic peptides with rat CSF in vitro and analysis of their products by HPLC demonstrated the presence in CSF of a peptidyl dipeptidase [peptidyl dipeptide hydrolase; angiotensin I converting enzyme (ACE); kininase II; EC 3.4.15.1] which sequentially degraded bradykinin (BK) by liberating the carboxy‐terminal ...
Shoichiro Nosaka
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Biochemical and Biophysical Research Communications, 1986
Cultured bovine pulmonary artery endothelial cells contain a second peptidyl dipeptidase, distinct from angiotensin-converting enzyme, present in an inactive form associated with a non-dialyzable inhibitor. Partial purification by glycine affinity chromatography separates enzyme from inhibitor to yield a preparation which hydrolyzes angiotensin-1 ...
J J Lanzillo +2 more
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Cultured bovine pulmonary artery endothelial cells contain a second peptidyl dipeptidase, distinct from angiotensin-converting enzyme, present in an inactive form associated with a non-dialyzable inhibitor. Partial purification by glycine affinity chromatography separates enzyme from inhibitor to yield a preparation which hydrolyzes angiotensin-1 ...
J J Lanzillo +2 more
exaly +3 more sources
, 2013