Brain Protein Kinase C Phosphorylating poly(Arginine,Serine) or Lamin B is Stimulated by Anions and by an Activator Purified from Bovine Serum Albumin Preparations

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 86; no. 6; pp. 1761 - 1765
• Main Authors: Abdel-Ghany, M., El-Gendy, K., Zhang, S., Raden, D., Racker, E.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01.03.1989; National Acad Sciences
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Anions; Antibodies; Biological and medical sciences; bovine serum albumin; brain; Brain - enzymology; Cell membranes; Cytosol; Enzyme Activation - drug effects; Fundamental and applied biological sciences. Psychology; Histones; Histones - metabolism; Humans; Isoenzymes - metabolism; Lamin Type B; Lamins; Lipids; Nuclear Proteins - metabolism; Peptides - metabolism; Phosphates - pharmacology; Phosphorylation; Placenta - analysis; Protein Kinase C - antagonists & inhibitors; Protein Kinase C - metabolism; Proteins; Rats; Serum Albumin, Bovine - analysis; Serum Albumin, Bovine - pharmacology; Serum albumins; Sheep; Substrate Specificity; Sulfates - pharmacology; Swine; Ungulates; Brain; Phosphorylation; Protein kinase C; Purification; Calcium; Radiolabelling; Rat; Gel electrophoresis; Serine; Rodentia; Lipids; Stimulation; Activation; Proteins; Vertebrata; Anions; Mammalia; Enzymatic activity; Arginine; Affinity chromatography; Inhibition; Histone

The phosphorylation of histone by purified protein kinase C (PK-C) from rat brain is dependent on the presence of Ca2+ and lipids. Phosphorylation of a synthetic random polymer of arginine and serine (3:1) is only moderately enhanced by Ca2+ and lipids, but it is greatly enhanced in the absence of C...