Studies on Cardiac Phosphoprotein Phosphatases

Li, Heng-Chun

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Heart, Lung, and Blood Institute (NHLBI)
• Type: Research Project (R01)
• Project #: 3R01HL022962-06S1
• Application #: 3337075
• Study Section: Biochemistry Study Section (BIO)
• Project Start: 1979-05-01
• Project End: 1986-02-28
• Budget Start: 1986-01-01
• Budget End: 1986-02-28
• Support Year: 6
• Fiscal Year: 1986

Institution

• Name: Mount Sinai School of Medicine
• Type: Schools of Medicine
• City: New York
• State: NY
• Country: United States
• Zip Code: 10029

Publications

Li, H C; Simonelli, P F; Huan, L J (1988) Preparation of protein phosphatase-resistant substrates using adenosine 5'-O-(gamma-thio)triphosphate. Methods Enzymol 159:346-56

Price, D J; Tabarini, D; Li, H C (1986) Purification, subunit composition and regulatory properties of the ATP X Mg2+-dependent form of type I phosphoprotein phosphatase from bovine heart. Eur J Biochem 158:635-45

Chernoff, J; Li, H C (1985) A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphatase. Arch Biochem Biophys 240:135-45

Li, H C; Price, D J; Tabarini, D (1985) On the mechanism of regulation of type I phosphoprotein phosphatase from bovine heart. Regulation by a novel intracyclic activation-deactivation mechanism via transient phosphorylation of the regulatory subunit by phosphatase-1 kinase (FA). J Biol Chem 260:6416-26

Price, D J; Li, H C (1985) Activation of bovine heart ATP-MG2+-dependent phosphoprotein phosphatase: isolation of a phosphoenzyme intermediate and its conversion to the active form via a Mg2+-dependent autodephosphorylation reaction. Biochem Biophys Res Commun 128:1203-10