ATP x Mg-dependent protein phosphatase from rabbit skeletal muscle. I. Purification of the enzyme and its regulation by the interaction with an activating protein factor.
TLDR
An ATP x Mg-dependent protein phosphatase (FC) was purified to near homogeneity from rabbit muscle and could be activated by a protein activator (FA) in the presence of ATP and Mg ions.About:
This article is published in Journal of Biological Chemistry.The article was published on 1980-12-25 and is currently open access. It has received 174 citations till now. The article focuses on the topics: Phosphatase & [phosphorylase] phosphatase activity.read more
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The role of protein phosphorylation in neural and hormonal control of cellular activity
TL;DR: There is an integrated network of regulatory pathways, mediated by phosphorylation–dephosphorylation, that allows diverse cellular events to be coordinated by neural and hormonal stimuli, and the evidence that supports this concept is reviewed.
Journal ArticleDOI
Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes
TL;DR: A hypothesis is proposed explaining how phosphatases might act synergistically with the kinases to elicit a full physiological response, without regard to the state of phosphorylation of the target proteins.
Journal ArticleDOI
Glycogen Synthase Kinase-3 from Rabbit Skeletal Muscle
TL;DR: This chapter discusses glycogen synthase kinase-3 from rabbit skeletal muscle, which has a second activity that is not shared by any other protein kinase—namely, the ability to activate an enzyme termed the MgATP-dependent protein phosphatase.
Journal ArticleDOI
Protein phosphatases: properties and role in cellular regulation
TL;DR: The properties, physiological roles, and mechanisms for regulating the four protein phosphatases are reviewed and their roles in controlling glycogen metabolism, glycolysis, gluconeogenesis, fatty acid synthesis, cholesterol synthesis, and protein synthesis are reviewed.
Journal ArticleDOI
The structure, role, and regulation of type 1 protein phosphatases.
Mathieu Bollen,Willy Stalmans +1 more
TL;DR: PP-1 plays an essential role in glycogen metabolism, calcium transport, muscle contraction, intracellular transport, protein synthesis, and cell division, and the activity of PP-1 is regulated by hormones like insulin, glucagon, alpha- and beta-adrenergic agonists, glucocorticoids, and thyroid hormones.
References
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Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
Klaus Weber,Mary Osborn +1 more
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
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A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein Mixtures
Robert G. Martin,Bruce N. Ames +1 more
TL;DR: Sucrose gradient centrifugation is found to be a suitable method for determining sedimentation coefficients of enzymes in protein mixtures and the sedimentation behavior of several of the enzymes in the pathway of histidine biosynthesis in S. typhimurium has been determined.
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Purification and Characterization of a Protein Inhibitor of Adenosine 3',5'-Monophosphate-dependent Protein Kinases
Donal A. Walsh,Charles D. Ashby,Carmen Gonzalez,Dianne F. Calkins,Edmond H. Fischer,Edwin G. Krebs +5 more
TL;DR: A kinetic analysis of the effect of the inhibitor on the phosphorylation of casein by skeletal muscle protein kinase indicates that it interacts noncompetitively with respect to ATP, the protein substrate, and adenosine 3',5'-monophosphate.