Results 101 to 110 of about 5,000 (140)
Some of the next articles are maybe not open access.

[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

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
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

[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

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

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

[Activity of peptidyl-dipeptidase A and carboxypeptidase N in the serum of patients with Alzheimer disease].

Ukrains'kyi biokhimichnyi zhurnal (1999 ), 2008
The activity of peptidyl-dipeptidase A and carboxypeptidase N taking part in peptide metabolism in the serum of patients with Alzheimer disease were studied. The role of these enzymes in the metabolism of neuropeptides and beta-amyloid at the Alzheimer disease was discussed.
V B, Solov'ev, M T, Gengin
openaire   +1 more source

Home - About - Disclaimer - Privacy