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Metabolic Interconversion of Enzymes 1980: International by O. Hayaishi, M. Kawaichi, N. Ogata, K. Ueda (auth.),

By O. Hayaishi, M. Kawaichi, N. Ogata, K. Ueda (auth.), Professor Dr. Helmut Holzer (eds.)

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Extra resources for Metabolic Interconversion of Enzymes 1980: International Titisee Conference October 1st – 5th, 1980

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The results demonstrate that two distinct protein phosphatase catalytic subunits are present in mammalian liver. Both enzymes have very similar physical properties and broad substrate specificities, but they can clearly be distinguished by the use of 11 ,1 2 and phosphorylase kinase. 15 M) and slightly earlier on Sephadex GlOO (M r = 34K vs Mr 33K). 9 Separation of Protein Phosphatase-2 into Several Subclasses A difference between the type-2 catalytic subunit present in preparations of protein phosphatase C from liver (M r =34K) and the PrP-2 described previously from rabbit skeletal muscle (M r = 170K) was that the former had a much higher activity ratio phosphorylase phosphatase/phosphorylase kinase phosphatase.

This enzyme could be separated from other phosphatases, which were fully active in the absence of ATP-Mg, by gel filtration or sucrose density gradient centrifugation. Goris et al. [58] subsequently resolved the ATP-Mg-dependent phosphorylase phosphatase into two components by chromatography on DEAE-cellulose, termed Fe and FA, both of which were required for activity. Fe, which has been partially purified from dog liver, is an inactive phosphatase, whereas FA is the activating factor [59]. The ATP-Mg-dependent phosphorylase phosphatase has been identified in liver, heart, and skeletal muscle from rats and rabbits, and similarly resolved into the Fe and FA components [60].

Type-l protein phosphatases dephosphorylate the fj-subunit of phosphorylase kinase and are potently inhibited by 11 and 12 , whereas type-2 protein phosphatases dephosphorylate the a-subunit of phosphorylase kinase and are insensitive to 11 and 12 , Two type-l protein phosphatases have been identified, namely PrP-! and the ATP-Mg-dependent protein phosphatase. The properties of these two enzymes are so similar that they may be interconvertible forms of the same enzyme. Three type-2 protein phosphatases have been identified, namely PrP-2b, PrP-2al, and PrP-2a2' The latter two enzymes share the same catalytic subunit but differ in that PrP-2a2 lacks one of the two additional subunits.

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