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  • 1
    Electronic Resource
    Electronic Resource
    Bradykinin inactivating enzymes in rabbit tissues: Sites of peptide bond hydrolysis (1976)
    Springer
    Inflammation research 6 (1976), S. 418-418 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01973217
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Endo-Oligopeptidase A., a Putative Enkephalin-Generating Enzyme, in the Vertebrate Retina (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 57 (1991), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: : Endo-oligopeptidase A., EC 3.4.22.19, converts small enkephalin-containing peptides into the corresponding enkephalins in vitro. We investigated the presence of endooligopeptidase A in the retina and its possible colocalization with enkephalins in retinal neurons. The specific activity of endo-oligopeptidase A found in pigeon retinae (30.3 ± 7.3 mU/mg, mean ± standard deviation) was four times higher than in rabbit retinae (7.0 ± 1.1 mU/mg). The enzyme activity was not modified by EDTA, but it was enhanced by dithiothreitol and inhibited by zinc and 5.5′-dithiobis(2-nitrobenzoic acid). Immunohistochemical experiments with a purified antiserum against rabbit endo-oligopeptidase A revealed labeled neurons in both the inner nuclear layer and the ganglion cell layer of pigeon and rabbit retinae. Double-labeling immunofluorescence experiments demonstrated that about 90% of neurons containing endo-oligopeptidase A-like immune-reactivity also contained [Leu5)-enkephalin-like immuno-reactivity. These colocalization results may represent an important step toward the demonstration of the possible involvement of endo-oligopeptidase A in enkephalin generation in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb06363.x
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  • 3
    Electronic Resource
    Electronic Resource
    Neuropeptide-Metabolizing Peptidases of Nervous Tissue (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 53 (1989), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1989.tb07332.x
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  • 4
    Electronic Resource
    Electronic Resource
    Involvement of Endo-Oligopeptidases A and B in the Degradation of Neurotensin by Rabbit Brain (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Incubation of neurotensin with rabbit brain cytosol fractions resulted in a rapid loss of carboxy-terminal neurotensin immunoreactivity, whereas the amino-terminal portion of neurotensin was relatively stable to degradation. Neurotensin degradation by rabbit brain cystosol fractions was activated by dithiothreitol and inhibited by thiol blocking reagents, Zn2 +, and by monospecific antibodies against endo-oligopeptidases A and B, thus suggesting the possible involvement of these enzymes in neurotensin degradation by rabbit brain. An association of a proportion of endo-oligopeptidase B activity (proline endo-peptidase) with the membrane fraction of nervous tissue was suggested by the presence of proline endopeptidase activity on the membranes and by immunoprecipitation of the solubilized activity using antiendo-oligopeptidase B antiserum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb12768.x
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  • 5
    Electronic Resource
    Electronic Resource
    BRAIN PEPTIDASES: CONVERSION AND INACTIVATION OF KININ HORMONES (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Two enzymes that selectively hydrolyse kinins at pH 7.5 were obtained in partially purified form from the supernatant fraction of homogenates of previously frozen rabbit brain by gel filtration on Sephadex G-100. The enzymes were detected and their activity estimated by bioassay with the isolated guinea pig ileum The products of the enzymic reactions were identified by high voltage electrophoresis at pH 3.5 and by the determination with the amino acid analyser of the amino acids released from the kinins.One enzyme, kinin-converting enzyme, catalyses the hydrolysis of kinin-10 (Lysbradykinin) and kinin-11 (Met-Lys-bradykinin) into kinin-9 (bradykinin). It also hydrolyses the aminoacyl-8-naphthylamides of methionine, lysine, arginine and leucine. The conversion of kinin-10 to kinin-9 was inhibited by puromycin (Ki 3.5 × 10−5 M) These properties are similar to those of brain arylamidases described in the literature.Kininase, the second enzyme, inactives kinins 9, 10 and 11 by peptide-bond hydrolysis. Similar rates of release of arginine and phenylalanine were observed for the three kinins, suggesting that kininase acts at the carboxy-terminus of these peptides.Our results suggest that brain contains proteases which apparently selectively metabolize polypeptide hormones that exert definite pharmacological effects on the central and peripheral nervous systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1972.tb01251.x
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  • 6
    Electronic Resource
    Electronic Resource
    The effect of partial hepatectomy upon circadian distribution of mitosis in the cornea of rats (1968)
    Springer
    Cellular and molecular life sciences 24 (1968), S. 569-570 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Die Resultate zeigen, dass der oder die Mechanismen, welche die Mitosis in der Cornea von normalen Tieren synchronisieren, nach partieller Hepatektomie immer noch aktiv sind.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02153777
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  • 7
    Electronic Resource
    Electronic Resource
    Bradykinin inactivation by perfused rat liver (1979)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 309 (1979), S. 197-201 
    Details
    ISSN: 1432-1912
    Keywords: Kinin inactivation ; Liver perfusion ; Endopeptidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Previous data had suggested the presence of at least two enzymes in the perfused rat liver — a peptidyldipeptide hydrolase (EC 3.4.15.1) which inactivates bradykinin (BK) and converts angiotensin I (AI) to angiotensin II (AII), and an enzyme which inactivates AII. However, in the present studies the amides of BK and bradykinylglycine were inactivated by the perfused liver at the same rate as BK suggesting that the inactivation of BK was due not only to the presence of the peptidyldipeptide hydrolase which requires a free carboxyl group but to an additional, as yet unidentified kininase. A 10-min perfusion of rat liver with oxygenated Tyrode solution containing 0.05% (v/v) Triton X-100 liberated significant amounts of kininase, potassium, lactic dehydrogenase and acid phosphatase into the perfusion medium. DEAE-cellulose chromatography of this perfusate purified the kininase activity, which does not hydrolyze either AI or AII. BK hydrolysis at pH 7.0 by this enzyme was inhibited by 1×10−3 M sodium tetrathionate but not by 3×10−3 M EDTA or BPP9a (10 μg/ml), a BK-potentiating nonapeptide which inhibits the peptidyldipeptide hydrolase. The endopeptidase splits BK between the Phe5-Ser6 bond forming the peptides Arg1-Phe5 and Ser6-Arg9 in stoichiometric amounts. It may be crucial for the BK inactivation by the perfused rat liver.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00501229
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  • 8
    Electronic Resource
    Electronic Resource
    Catabolism of vasoactive polypeptides by perfused rat liver (1976)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 295 (1976), S. 33-40 
    Details
    ISSN: 1432-1912
    Keywords: Kinin inactivation ; Angiotensin inactivation ; Angiotensin conversion ; Liver perfusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Exsanguinated rat liver preparations perfused in situ with oxygenated saline solutions inactivated recirculating bradykinin (BK) at rates of 2.3 to 9.1 and isoleucyl5 angiotensin II (AII) at rates of 2.8 to 15.0 nmolex x min−1 x g−1 of liver, depending on the initial concentration of the peptides in the perfusion fluid (3.1 to 18.9×10−6 M for BK and 8.5 to 17.0×10−6M for AII). On the other hand, at similar concentrations, recirculation of isoleucyl5 Angiotensin I (AI) for 8 min did not lead to decrease of its biological activity when assayed on the isolated rat uterus. Following a single passage through liver, picomole amounts of both BK and AII were inactivated by about 90% as revealed by assays on a superfused rat uterus. The potency ratio AI:AII, assayed on a superfused rat uterus was 1:22 and changed to 1:5 following a single passage of both peptides through liver. This finding and the separation of 4.9% of AII on carboxymethylcellulose columns following recirculation of AI through rat liver indicate a conversion of AI into AII. The dipeptides Phe-Arg, Ser-Pro and Gly-Phe were identified among the hydrolysis products of perfused BK. A peptidyldipeptide hydrolase (EC 3.4.15) may be responsible for both the BK inactivation and AI conversion. The inactivation of AII cannot be attributed to the same enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00509769
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  • 9
    Electronic Resource
    Electronic Resource
    Cross examination of the conformational spaces of a set of peptide chains: Study of oligopeptidase action (1996)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 60 (1996), S. 1815-1827 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A conformational search was carried out for five opioid peptide homologues and for angiotensin II. Density of states versus energy plots were obtained for each peptide, and the occurrence of common main-chain conformations was investigated by searching homologies between strings of four, five, and six contiguous main-chain amino acid residues rotamers. The results were compared to rates of hydrolysis by endooligopeptidase (EOP) 24.15, known for its specificity for substrate conformations. A catalytic assay of the hydrolysis of angiotensin II was also performed. The two best substrates of EOP 24.15 were found to share unique main-chain conformations and the two worst substrates of EOP 24.15 were found to be nonstructurally homologous to each other and the remaining peptide chains. The conformational search is compared to previous experimental and theoretical results. © 1996 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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