Abstract
A nucleoside triphosphatase (NTPase) activity appeared to be associated with a highly purified nuclear preparation from rat cardiac ventricles. Different nucleoside triphosphates (UTP > GTP > ITP > CTP) supported this enzymic activity, which was stimulated by Mg` but not by Call. The nuclear NTPase activity could be down regulated by endogenous phosphorylation of a 55,000 Mr protein. Maximal phosphorylation of the 55,000 Mr protein occurred in the presence of Mg2+-ATP. Addition of cAMP, cGMP, Ca2+, Ca2+/phospholipid, Ca2+/calmodulin, and catalytic subunit of cAMP-dependent protein kinase was not associated with any further phosphorylation of the 55,000 Mr protein. However, in the presence of Ca2+/calmodulin or the catalytic subunit of the cAMP-dependent protein kinase additional proteins became phosphorylated, but these had no effect on the Mg2+-NTPase activity. These results indicate that a protein with Mr 55,000 may be involved in the regulation the Mg2+-NTPase activity associated with rat cardiac nuclei.
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Abbreviations
- Hg:
-
Hemoglobin
- GAR:
-
Goat Anti-Rabbit antibody
- SR:
-
Sarcoplasmic Reticulum
- NTP:
-
Nucleoside Triphosphate
- TCA:
-
Trichloroacetic acid
- PAGE:
-
Polyacrylamide gel electrophoresis
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Gupta, R.C., Young, E.F., Ferguson, D.G. et al. Regulation of rat cardiac nuclei-associated Mg2+-NTPase by phosphorylation. Mol Cell Biochem 102, 165–172 (1991). https://doi.org/10.1007/BF00234574
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DOI: https://doi.org/10.1007/BF00234574