PubMed:3921407 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/3921407","sourcedb":"PubMed","sourceid":"3921407","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/3921407","text":"Phosphoprotein phosphatase inhibitor-2 is phosphorylated at both serine and threonine residues in mouse diaphragm.\nPhosphoprotein phosphatase inhibitor-2 (i-2) was rapidly isolated from mouse diaphragm extracts by the use of specific antibodies. The i-2 so obtained was associated with ATP-Mg and FA/GSK-3 dependent phosphatase activity, supporting the idea that i-2 is in fact a component of this form of phosphatase. Inhibitor-2 isolated from diaphragms incubated with [32P]phosphate contained both phosphoserine (approximately 90%) and phosphothreonine (approximately 10%). 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