Distribution of endogenously phosphorylated proteins in subcellular fractions of rat cerebral cortex

1977 ◽  
Vol 2 (5) ◽  
pp. 533-548 ◽  
Author(s):  
Yigal H. Ehrlich ◽  
Leonard G. Davis ◽  
Thomas Gilfoil ◽  
Eric G. Brunngraber
Keyword(s):  
Cerebral Cortex ◽  
Subcellular Fractions ◽  
Rat Cerebral Cortex ◽  
Phosphorylated Proteins

scholarly journals Pre-incubation of subcellular fractions from rat cerebral cortex inactivates protein phosphorylation

1981 ◽  
Vol 199 (1) ◽  
pp. 269-272 ◽  
Author(s):  
P R Dunkley ◽  
P J Robinson
Keyword(s):  
Cerebral Cortex ◽  
Cyclic Amp ◽  
Protein Phosphorylation ◽  
Rat Brain ◽  
Subcellular Fractions ◽  
Rat Cerebral Cortex ◽  
Substrate Availability ◽  
Physiological Relevance

Pre-incubation of various subcellular fractions from rat brain caused a significant decrease in the phosphorylation of individual polypeptides. The rate and extent of this loss of labelling was not uniform and polypeptides whose phosphorylation was independent of cyclic AMP were primarily affected, whereas substrate availability remained unaltered. It is recommended that pre-incubation effects must be carefully monitored if valid conclusions are to be made about the physiological relevance of changes in protein phosphorylation observed in vitro.

scholarly journals The diglyceride kinase of rat cerebral cortex

1971 ◽  
Vol 122 (2) ◽  
pp. 171-179 ◽  
Author(s):  
E. G. Lapetina ◽  
J. N. Hawthorne
Keyword(s):  
Cerebral Cortex ◽  
Phosphatidic Acid ◽  
Nerve Ending ◽  
Osmotic Shock ◽  
Sodium Deoxycholate ◽  
Acid Synthesis ◽  
Optimum Concentration ◽  
Subcellular Fractions ◽  
Rat Cerebral Cortex ◽  
Triton X

1. Formation of phosphatidic acid by diglyceride kinase (EC 2.7.1.-) in the presence of ATP and Mg2+ was shown in a homogenate and subcellular fractions of rat cerebral cortex. 2. The kinase was activated by Mg2+. Ca2+ activated to a smaller extent but was inhibitory in the presence of optimum concentration of Mg2+. Activity was greatly increased in the presence of added 1,2-diglyceride. 3. Sodium deoxycholate markedly stimulated the reaction, but other detergents (Cutscum and Triton X-100) did not. 4. Diglyceride kinase was concentrated in the supernatant and microsomal fractions from rat cerebral cortex. The distribution of the kinase in the particulate fractions resembled that of acetylcholinesterase and 5′-nucleotidase. 5. The rate of phosphatidic acid synthesis by the diglyceride kinase route was much greater than reported rates for acylation of 3-glycerophosphate and was also very rapid in comparison with the rates of other steps in the synthesis of phosphoinositides. 6. Acetylcholine had no stimulatory effect on diglyceride kinase of isolated intact nerve-ending particles or of nerve-ending membranes obtained after osmotic shock.

Turnover of proteins in subcellular fractions of rat cerebral cortex

1971 ◽  
Vol 31 (1) ◽  
pp. 179-184 ◽  
Author(s):  
Georgina Rodríguez de Lores Arnaiz ◽  
Martha Alberici de Canal ◽  
Eduardo de Robertis
Keyword(s):  
Cerebral Cortex ◽  
Subcellular Fractions ◽  
Rat Cerebral Cortex
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