These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: GTP-sensitive phosphorylation of proteins in a postmitochondrial supernatant from rat brainstem affected by ACTH1-24.
    Author: Van Dijk AM, King GB, Schotman P, Gispen WH.
    Journal: Neurochem Res; 1981 Aug; 6(8):847-61. PubMed ID: 6273759.
    Abstract:
    The effect of ACTH1-24 and cyclic nucleotides on the endogenous phosphorylation of proteins from a postmitochondrial supernatant from rat brainstem was investigated in the presence and absence of GTP. Phosphorylation and its modulation by these compounds were studied in vitro by incorporation of labeled phosphate from [gamma-32P]ATP added to the incubation mixture. Phosphoproteins were subsequently analyzed by autoradiography after one- and two-dimensional separation. Eight ACTH-sensitive phosphoproteins of molecular weights 75 (IEP 4.0), 67, 64, 50 (IEP 4.7), 47 (IEP 4.8), 38, 34, and 24K were found. The effects of ACTH on phosphorylation were mainly inhibitory, and the affected protein bands did not coincide with the phosphoproteins sensitive to cyclic AMP and cyclic GMP. Phosphorylation of those phosphoprotein bands and its ACTH sensitivity appeared to be highly sensitive to GTP. It is suggested that the activity of protein kinases involved in hormone-sensitive phosphorylation in a postmitochondrial rat brainstem fraction is regulated by GTP-dependent mechanisms.
    [Abstract] [Full Text] [Related] [New Search]