Results 151 to 160 of about 6,534 (185)
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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
openaire   +2 more sources

[Peptides--inhibitors of carboxycathepsin (peptidyl-dipeptidase A) and their role in clinical medicine].

Voprosy meditsinskoi khimii, 1984
Properties of the carboxycathepsin inhibitors teprotide, captopryl, enalacryl are considered. Presence of low molecular thermo- and acid stable carboxycathepsin inhibitors of peptide nature in blood serum and lymphocytes is discussed.
V N, Orekhovich   +4 more
openaire   +3 more sources

A peptidyl dipeptidase-4 from Pseudomonas maltophilia: Purification and properties

Archives of Biochemistry and Biophysics, 1989
A peptidyl dipeptidase-4 (bacterial PDP-4) was purified to near homogeneity from a supernatant of Pseudomonas maltophilia extracellular medium. Bacterial PDP-4 is a single-polypeptide-chain enzyme, 82 kDa, with an alkaline isoelectric point. Peptides susceptible to hydrolysis by bacterial PDP-4 include angiotensin 1, bradykinin, enkephalins ...
Y, Dasarathy   +3 more
openaire   +2 more sources

Preferential action of rat brain cathepsin B as a peptidyl dipeptidase converting pro-opioid oligopeptides

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.
N, Marks, M J, Berg, M, Benuck
openaire   +2 more sources

Purification and Characterization of a Peptidyl Dipeptidase Resembling Angiotensin Converting Enzyme from the Electric Organ of Torpedo marmorata

Journal of Neurochemistry, 1987
Abstract: The electric organ of Torpedo marmorata contains a membrane‐bound, captopril‐sensitive metallopepti‐dase that resembles mammalian angiotensin converting enzyme (peptidyl dipeptidase A; EC 3.4.15.1). The Torpedo enzyme has now been purified to apparent homogeneity from electric organ by a procedure involving affinity chro‐matography using the
A J, Turner   +3 more
openaire   +2 more sources

The isolation of a peptidyl dipeptidase from mouse brain cytosol that cleaves adrenocorticotropic hormone-(7–10) and des-tyrosine-enkephalins

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.
A, Neidle, J A, Kelly
openaire   +2 more sources

[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.
L V, Pavlikhina   +3 more
openaire   +1 more source

Prodynorphin processing by rat CNS fractions and purified enzymes: Formation of Dynorphin A 1–8 by sulfhydryl-activated carboxypeptidase and peptidyl dipeptidase

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.
N, Marks   +5 more
openaire   +2 more sources

Peptidyl dipeptidases (Ance and Acer) of Drosophila melanogaster: major differences in the substrate specificity of two homologs of human angiotensin I-converting enzyme

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.
Siviter, Richard J.   +5 more
openaire   +2 more sources

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