The use of phosphopeptides to distinguish between protein phosphatase and acid/alkaline phosphatase activities: opposite specificity toward phosphoseryl/phosphothreonyl substrates-Reference-Cited by-同舟云学术

The use of phosphopeptides to distinguish between protein phosphatase and acid/alkaline phosphatase activities: opposite specificity toward phosphoseryl/phosphothreonyl substrates

Published:1991-08 Issue:1 Volume:1094 Page:130-133
ISSN:0167-4889
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Author:

Donella-Deana Arianna,Meyer Helmut E.,Pinna L.A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference24 articles.

1. THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASES

2. Purification and properties of polycation-stimulated phosphorylase phosphatases from rabbit skeletal muscle.

3. Dephosphorylation of phosphoproteins and synthetic phosphopeptides. Study of the specificity of the polycation-stimulated and MgATP-dependent phosphorylase phosphatases.

4. Synthetic peptides as model substrates for the study of the specificity of the polycation-stimulated protein phosphatases

5. An investigation of the substrate specificity of protein phosphatase 2C using synthetic peptide substrates; comparison with protein phosphatase 2A

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