Results 141 to 150 of about 6,496 (160)
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A distinct peptidyl dipeptidase that degrades enkephalin: Exceptionally high activity in rabbit kidney

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, M J, Berg, N, Marks
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[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
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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
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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
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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
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Conversion of angiotensin-1 to angiotensin-2 by a latent endothelial cell peptidyl dipeptidase that is not angiotensin-converting enzyme

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   +3 more
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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
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Membrane Localization of Endopeptidase‐24.11 and Peptidyl Dipeptidase A (Angiotensin Converting Enzyme) in the Pig Brain: A Study Using Subcellular Fractionation and Electron Microscopic Immunocytochemistry

Journal of Neurochemistry, 1992
Abstract: Brains from piglets were dissected and a block of tissue including the substantia nigra, globus pallidus, and entopeduncular nucleus was homogenized and then fractionated on discontinuous Percoll gradients. Ligand‐binding assays using (–)‐[3H]nicotine and [3H]quinuclidinyl benzilate served to delineate fractions containing nicotinic and ...
K, Barnes, A J, Turner, A J, Kenny
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Peptidyl Dipeptidase A-Catalyzed Metabolism of Delta Sleep-Inducing Peptide in Bovine Brain Microvessel Endothelial Cells: A Cell Culture Model of the Blood-Brain Barrier

Biochemical and Biophysical Research Communications, 1995
Previous studies have shown that the metabolism of delta sleep-inducing peptide (DSIP) in the blood-brain barrier (BBB) is catalyzed by amino-peptidases. In this study, we have shown that peptidyl dipeptidase A in cultured bovine brain microvessel endothelial cells (BBMEC), a model of the BBB, and a purified form of this enzyme can also metabolize DSIP
P F, Augustijns   +3 more
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Some Characteristics of a Peptidyl Dipeptidase (Kininase II) from Rat CSF: Differential Effects of NaC1 on the Sequential Degradation Steps of Bradykinin

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 ...
Takeshi Yoshida, Shoichiro Nosaka
openaire   +1 more source

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