T
Thomas J. Lynch
Researcher at St. Jude Children's Research Hospital
Publications - 12
Citations - 923
Thomas J. Lynch is an academic researcher from St. Jude Children's Research Hospital. The author has contributed to research in topics: Phosphodiesterase & Cyclase. The author has an hindex of 10, co-authored 12 publications receiving 923 citations. Previous affiliations of Thomas J. Lynch include University of Houston & University of Tennessee.
Papers
More filters
Journal ArticleDOI
Protein activator of cyclic 3':5'-nucleotide phosphodiesterase of bovine or rat brain also activates its adenylate cyclase.
TL;DR: Findings indicate that brain adenylate cyclase required an activator for activity and that this activator is functionally identical to the protein activator of phosphodiesterase (J.B.C. 249: 4943–4954, 1974).
Journal ArticleDOI
Purification and characterization of an inhibitor protein of brain adenylate cyclase and cyclic nucleotide phosphodiesterase.
TL;DR: A heat-labile inhibitor protein of adenylate cyclase and phosphodiesterase has been purified to apparent homogeneity from bovine brain cerebrum by a simple two-column procedure and the thermal stability of the inhibitor was increased, indicative of a new conformation.
Journal ArticleDOI
Human erythrocyte Ca2+-Mg2+-ATPase: mechanism of stimulation by Ca2+.
Thomas J. Lynch,Wai Yiu Cheung +1 more
TL;DR: The mode of stimulation of human erythrocyte Ca2+-Mg2--ATPase by calmodulin appears similar to that of Ca2-dependent adenylate cyclase and phosphodiesterase.
Journal ArticleDOI
Ca++-dependent formation of brain adenylate cyclase-protein activator complex
TL;DR: The results suggest that the formation of the enzyme-activator complex is dependent on Ca++, and that adenylate cyclase activityin vivo could be modulated by the cellular flux of Ca++.
Journal ArticleDOI
Rat brain adenylate cyclase. Further studies on its stimulation by a Ca2+-binding protein.
TL;DR: It is shown that particulate rat brain adenylate cyclase also required the Ca2+-binding protein activator for maximum activity, and results suggest that the action of the activator is independent of the other two ligands.