Regulatory effects of S-100 protein and parvalbumin on protein kinases and phosphoprotein phosphatases from brain and skeletal muscle

✍ Scribed by Wu-Nan Kuo; Thomas Blake; Ijaz R. Cheema; Jorge Dominguez; James Nicholson; Katia Puente; Phaedra Shells; Jimmie Lowery

• Publisher: Springer
• Year: 1986
• Tongue: English
• Weight: 356 KB
• Volume: 71
• Category: Article
• ISSN: 0300-8177
• DOI: 10.1007/bf00219324

✦ Synopsis

In the eluted fractions of histone-treated crude extracts separated by Sephadex G-200 filtration, multiple protein kinase (PK) activities, including three from brain and two from skeletal muscle, were augmented by both S-100 protein and parvalbumin on the phosphorylation of endogenous substrates. One additional PK activity suppressed by both S-100 and parvalbumin was also found in muscle. In comparison, phosphoprotein phosphatases (PPase), which were also prepared by the same procedure of initial step of histone-treatment followed by the steps of Bio-Gel P-6DG for brain and DNA-cellulose for muscle, were all activated by S-100 while inhibited by parvalbumin and phosphatidylserine.