| Literature DB >> 1848859 |
R E Honkanen1, J Zwiller, S L Daily, B S Khatra, M Dukelow, A L Boynton.
Abstract
A novel serine/threonine protein phosphatase is identified, and the catalytic subunit, obtained from a detergent extraction of the pellet generated by a 100,000 x g centrifugation of a whole bovine brain homogenate, is purified and characterized. The protein phosphatase, designated as PP3, has a Mr of 36,000, does not require divalent cations for activity, is stimulated rather than inhibited by inhibitor 2, is inhibited by both okadaic acid and microcystin-LR with an intermediate IC50 compared to type 1 and type 2A protein phosphatases, and preferentially dephosphorylates the beta subunit of phosphorylase kinase. Substrate specificity, immunoblotting with type-specific antisera, and the amino acid sequences of peptides derived from PP3 indicate that PP3 is not an isoform of any known serine/threonine protein phosphatase.Entities:
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Year: 1991 PMID： 1848859
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157