Results 141 to 150 of about 10,632 (177)
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Peptidyl-dipeptidase A/angiotensin I-converting enzyme
, 2013 Edward D. Sturrock +2 more
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Peptidyl-dipeptidase A/angiotensin I-converting enzyme
, 2004 P, Corvol, T A, Williams, F, Soubrier
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Bulletin of Experimental Biology and Medicine, 1985
L. P. Alekseenko, V. N. Orekhovich
exaly +2 more sources
L. P. Alekseenko, V. N. Orekhovich
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EFFECT OF PEPTIDYL‐DIPEPTIDASE INHIBITORS IN EXPERIMENTAL CONVULSIONS IN MICE
Fundamental & Clinical Pharmacology, 1987Summary— 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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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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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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A peptidyl dipeptidase-4 from Pseudomonas maltophilia: Purification and properties
Archives of Biochemistry and Biophysics, 1989A 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
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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.
N, Marks, M J, Berg, M, Benuck
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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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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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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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