Nitric oxide activation of soluble guanylyl cyclase reveals high and low affinity sites that mediate allosteric inhibition by calcium.

Kazerounian, Shiva; Pitari, Giovanni M; Ruiz-Stewart, Inez; Schulz, Stephanie; Waldman, Scott A

Kazerounian, Shiva; Pitari, Giovanni M; Ruiz-Stewart, Inez; Schulz, Stephanie; Waldman, Scott A.

Affiliation

Kazerounian S; Division of Clinical Pharmacology, Department of Medicine and Biochemistry, Thomas Jefferson University, Philadelphia, PA 19107, USA.

Biochemistry ; 41(10): 3396-404, 2002 Mar 12.

Article in En | MEDLINE | ID: mdl-11876648

Subject(s)

Calcium/physiology; Guanylate Cyclase/metabolism; Nitric Oxide/physiology; Allosteric Regulation; Animals; Binding Sites; Binding, Competitive; Cattle; Enzyme Activation; Kinetics; Lung/enzymology; Nitric Oxide Donors/pharmacology; Nitroprusside/pharmacology

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Collection: 01-internacional Database: MEDLINE Main subject: Calcium / Guanylate Cyclase / Nitric Oxide Limits: Animals Language: En Journal: Biochemistry Year: 2002 Document type: Article Affiliation country: United States Country of publication: United States

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