Results 141 to 150 of about 113,934,450 (165)
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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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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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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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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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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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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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[Determination of carboxycathepsin (peptidyl dipeptidase) activity in human blood serum].
Voprosy meditsinskoi khimii, 1975Based 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
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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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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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[37] Human peptidyl dipeptidase (converting enzyme, kininase II)
1981Tess A. Stewart +2 more
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Hydrolysis of Enkephalin by Cultured Human Endothelial Cells and by Purified Peptidyl Dipeptidase
1977Nit T. Boyden +2 more
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