Patrick E. Ward
Ohio State University
18 Papers
384 Citations
Patrick E. Ward is an academic researcher from Ohio State University. The author has contributed to research in topics: Amastatin & Bradykinin. The author has an hindex of 15, co-authored 18 publications.
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Papers
Metabolism of vasoactive peptides by plasma and purified renal aminopeptidase M
TL;DR: A significant role for vascular and plasma AmM in the metabolism of circulating vasoactive peptides is supported and comparative studies with the purified enzyme, immunoreactive AmM accounted for essentially all of the alanyl-2-naphthylamidase activity of rabbit plasma.
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•Journal Article
Dipeptidyl(amino)peptidase IV and aminopeptidase M metabolize circulating substance P in vivo.
TL;DR: In this paper, the absence of DAP IV was not associated with any differences in angiotensin-converting enzyme-mediated hydrolysis of SP (1.45 +/- 0.06 nmol/min/ml), due to a complete lack of dipeptidyl(amino)peptidine IV hydrolytic activity.
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Differential processing of substance P and neurokinin A by plasma dipeptidyl(amino)peptidase IV, aminopeptidase M and angiotensin converting enzyme.
Linhong Wang,Saleem Ahmad,Ibrahim F. Benter,Ana Chow,Shigehiko Mizutani,Shigehiko Mizutani,Patrick E. Ward +6 more
TL;DR: Differential processing of SP and NKA by specific peptidases in rat and human plasma is demonstrated.
87
Thrombin receptor activating peptides: importance of the N-terminal serine and its ionization state as judged by pH dependence, nuclear magnetic resonance spectroscopy, and cleavage by aminopeptidase M
Barry S. Coller,Patrick E. Ward,Marco Ceruso,Lesley E. Scudder,Karen T. Springer,Jeffery L. Kutok,Glenn D. Prestwich +6 more
TL;DR: Induction of platelet aggregation by these two peptides showed an unusual pH dependence, being more potent at pH 7.2 than at pH 8.1; thrombin-induced aggregation showed a reverse pH dependence.
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Metabolism of bradykinin analogs by angiotensin I converting enzyme and carboxypeptidase N
TL;DR: Data indicate an important role for plasma CPN and vascular CPN-like activity in the metabolism of the widely used ACE-resistant/D-Phe7-containing antagonists of B2 kinin receptors.
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