Results 141 to 150 of about 6,277 (184)
EFFECT OF PEPTIDYL‐DIPEPTIDASE INHIBITORS IN EXPERIMENTAL CONVULSIONS IN MICE
Fundamental & Clinical Pharmacology, 1987 Summary— 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
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Neurochemistry International, 1987 The conversion of selected prodynorphin fragments to form the octapeptide Dynorphin A 1-8 was studied in rat brain or spinal cord fractions, and the results compared to the action of purified carboxypeptidases and angiotension converting enzyme.
Neville Marks +5 more
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Amino acid residues essential for catalysis by peptidyl dipeptidase-4 from pseudomonas maltophilia
Biochemical and Biophysical Research Communications, 1989 To 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
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Hydrolysis of enkephalin by cultured human endothelial cells and by purified peptidyl dipeptidase
Biochemical Pharmacology, 1978 Abstract : 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. Erdös +2 more
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Peptides, 2002 Drosophila melanogaster angiotensin converting enzyme (Ance) and angiotensin converting enzyme related (Acer) are single domain homologs of mammalian peptidyl dipeptidase A (angiotensin I-converting enzyme) whose physiological substrates have not as yet been identified.
Richard J. Siviter +5 more
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Archives of Biochemistry and Biophysics, 1986 Purified rat brain cathepsin B (EC 3.4.22.1) converted prodynorphins or proenkephalins to shorter active forms by the preferential removal of C-terminal dipeptides. The substrate affinities for Met-enkephalin-Arg-Phe or -Arg-Gly-Leu were Km 46 and 117 microM, and kcat/Km ratios were 67 and 115 microM-1, min-1, respectively.
Neville Marks, Martin J. Berg, M. Benuck
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[37] Human peptidyl dipeptidase (converting enzyme, kininase II)
, 1981 Publisher Summary This chapter presents the procedure for the large-scale purification of membrane-bound human lung and kidney converting enzyme (CE). 13 mg of homogeneous enzyme is obtained from 15.8 kg of lung tissue, and 29 mg of enzyme from 5.8 kg of kidney. About half the enzyme content of the cadaver lung goes into solution after homogenization;
T.A. Stewart +2 more
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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 ...
Joseph J. Lanzillo +3 more
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Archives of Biochemistry and Biophysics, 1984 An enzyme present in mouse brain cytosol cleaves C-terminal dipeptides from substrates including ACTH-(7-10) (Phe-Arg-Trp-Gly), and des-Tyr-[Met]- and des-Tyr-[Leu]enkephalin. By means of ion-exchange chromatography and gel filtration, the peptidase was purified to a specific activity of 1570 times that of brain homogenate.
Amos Neidle, Julie Kelly
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[Determination of carboxycathepsin (peptidyl dipeptidase) activity in human blood serum].
Voprosy meditsinskoi khimii, 1975 Based on fluorometric determination of a dipeptide histidil-leucine, which is splitted off from a synthetic substrate (Cbz-Phe-His-Leu) by carboxycathepsin (carboxydipeptidyl peptide hydrolase), a method was developed for estimation of the enzymatic activity in human blood serum.
Pavlikhina Lv +3 more
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