Abstract:
: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.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Kuo WN,Blake T,Cheema IR,Dominguez J,Nicholson J,Puente K,Shells P,Lowery Jdoi
10.1007/BF00219324subject
Has Abstractpub_date
1986-06-01 00:00:00pages
19-24issue
1eissn
0300-8177issn
1573-4919journal_volume
71pub_type
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