Zobrazeno 1 - 10
of 75
pro vyhledávání: '"A T, Orawski"'
Aminopeptidase P isozyme expression in human tissues and peripheral blood mononuclear cell fractions
Publikováno v:
Archives of Biochemistry and Biophysics. 435:303-310
Aminopeptidase P (APP) isoforms specifically remove the N-terminal amino acid from peptides that have a proline residue in the second position. The mRNA levels of three different isoforms, each coded by a different gene, were determined in 16 human t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f5e84199f3202ea5e10561d1121c0ac
https://doi.org/10.1016/j.abb.2004.12.023
https://doi.org/10.1016/j.abb.2004.12.023
Autor:
Arthur T. Orawski, William H. Simmons
Publikováno v:
Neurochemical Research. 17:817-820
The neuropeptide kyotorphin (Tyr-Arg) was degraded by rat brain synaptosomes via a synaptic membrane-bound peptidase which was inhibited by bestatin but not by amastatin. The Km for kyotorphin was 8 x 10(-6) M and the Ki for bestatin was 1 x 10(-7) M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e892259b2fe5222636bc5ef269ca9209
https://doi.org/10.1007/bf00969018
https://doi.org/10.1007/bf00969018
Autor:
A T Orawski, William H. Simmons
Publikováno v:
Journal of Biological Chemistry. 267:4897-4903
The membrane-bound form of aminopeptidase P (aminoacylprolyl-peptide hydrolase) (EC 3.4.11.9) was purified to apparent homogeneity from bovine lung microsomes. The enzyme was solubilized using phosphatidylinositol-specific phospholipase C (Bacillus t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c9ad227d97b4539a62516e808b3cfd0c
https://doi.org/10.1016/s0021-9258(18)42915-8
https://doi.org/10.1016/s0021-9258(18)42915-8
Publikováno v:
Peptides for the New Millennium ISBN: 0792364457
Aminopeptidase P inactivates bradykinin by hydrolyzing the bond [1]. This enzyme is a metallo-aminopeptidase with specificity for proline in the penultimate position. An inhibitor of this enzyme was synthesized and called apstatin (N-[(2S,3R)-3amino-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c851a2fc113de6a54cb38da2ae36bf49
https://doi.org/10.1007/0-306-46881-6_170
https://doi.org/10.1007/0-306-46881-6_170
Publikováno v:
Journal of medicinal chemistry. 42(13)
Membrane-bound aminopeptidase P (AP-P) participates in the degradation of bradykinin in several vascular beds. We have developed an inhibitor of AP-P called apstatin (1) (N-[(2S, 3R)-3-amino-2-hydroxy-4-phenyl-butanoyl]-L-prolyl-L-prolyl-L-al aninam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96b2ee4e1515fabfc9df29f16aa71287
https://pubmed.ncbi.nlm.nih.gov/10395480
https://pubmed.ncbi.nlm.nih.gov/10395480
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 275(3)
Bradykinin (Bk), a potent vasoactive and cardioprotective peptide hormone, is almost completely inactivated during a single circulation through the rat lung. It has been hypothesized that membrane-bound aminopeptidase P, which can hydrolyze the Arg1-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2b02d77078709a0a0bc1bd19ae75fb1c
https://pubmed.ncbi.nlm.nih.gov/8531074
https://pubmed.ncbi.nlm.nih.gov/8531074
Autor:
William H. Simmons, Arthur T. Orawski
Publikováno v:
Biochemistry. 34(35)
The membrane-bound form of aminopeptidase P (aminoacylprolyl-peptide hydrolase) (EC 3.4.11.9) was purified 670-fold to apparent homogeneity from rat lung microsomes. The enzyme was solubilized from the membranes using a phosphatidylinositol-specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9f9edf16a8782adbb9aea4b1472c3b8
https://pubmed.ncbi.nlm.nih.gov/7669781
https://pubmed.ncbi.nlm.nih.gov/7669781
Publikováno v:
Archives of biochemistry and biophysics. 311(1)
The substrate specificity of recombinant E. coli aminopeptidase P (aminoacylprolylpeptide hydrolase) (EC 3.4.11.9) was studied using about 150 synthetic peptides. E. coli aminopeptidase P released the N-terminal amino acid from most peptides containi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e2e8593721d86866448720c857b2fab
https://pubmed.ncbi.nlm.nih.gov/8185318
https://pubmed.ncbi.nlm.nih.gov/8185318
Autor:
W H, Simmons, A T, Orawski
Publikováno v:
The Journal of biological chemistry. 267(7)
The membrane-bound form of aminopeptidase P (aminoacylprolyl-peptide hydrolase) (EC 3.4.11.9) was purified to apparent homogeneity from bovine lung microsomes. The enzyme was solubilized using phosphatidylinositol-specific phospholipase C (Bacillus t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::47e11011a280c7983c412f0fd47a4558
https://pubmed.ncbi.nlm.nih.gov/1537867
https://pubmed.ncbi.nlm.nih.gov/1537867
Autor:
A T, Orawski, W H, Simmons
Publikováno v:
Agents and actions. Supplements. 38
Aminopeptidase P that hydrolyzes the Arg1-Pro2-bond of bradykinin was solubilized from rat lung microsomes using phosphatidylinositol-specific phospholipase C. The enzyme was purified 420-fold by chromatography on decylagarose (two steps), omega-amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f492a9859a14c09fe662cc70c7a6ca5d
https://pubmed.ncbi.nlm.nih.gov/1361300
https://pubmed.ncbi.nlm.nih.gov/1361300