Partial purification and characterization of sodium channel phosphatases from rat brain: Similarity to phosphatase 2A

Persistent Link:
http://hdl.handle.net/10150/278004
Title:
Partial purification and characterization of sodium channel phosphatases from rat brain: Similarity to phosphatase 2A
Author:
Chen, Tzu-chin, 1965-
Issue Date:
1991
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Four distinct serine/threonine protein phosphatases have been purified from and identified in various tissues. They are type 1 and type 2 phosphatases, which are further classified as phosphatase 2A, 2B, and 2C. In this study, endogenous brain phosphatases that dephosphorylate sodium channels were partially purified and characterized. Multiple peaks of sodium channel phosphatase were detected after DEAE-Sephadex chromatography and gel filtration. All peaks were sensitive to a low concentration of okadaic acid (10 nM), which strongly suggests that phosphatase 2A is the major brain phosphatase dephosphorylating sodium channels. Individual fractions containing sodium channel phosphatase activity from both DEAE-Sephadex chromatography and gel filtration were subjected to immunoblot with anti-phosphatase 2Ac antibody. The results indicate that all fractions containing phosphatase activity also contained phosphatase 2Ac immunoreactivity. The fractions which stained most intensely in the immunoblots were the fractions containing the highest phosphatase activity in all cases. The molecular weights of the multiple sodium channel phosphatases estimated by gel filtration were 83 kDa, 147 kDa, and 141 kDa. These may represent isozymes of phosphatase 2A in brain.
Type:
text; Thesis-Reproduction (electronic)
Keywords:
Health Sciences, Toxicology.; Health Sciences, Pharmacology.; Chemistry, Biochemistry.
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Graduate College
Degree Grantor:
University of Arizona
Advisor:
Rossie, Sandra S.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titlePartial purification and characterization of sodium channel phosphatases from rat brain: Similarity to phosphatase 2Aen_US
dc.creatorChen, Tzu-chin, 1965-en_US
dc.contributor.authorChen, Tzu-chin, 1965-en_US
dc.date.issued1991en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractFour distinct serine/threonine protein phosphatases have been purified from and identified in various tissues. They are type 1 and type 2 phosphatases, which are further classified as phosphatase 2A, 2B, and 2C. In this study, endogenous brain phosphatases that dephosphorylate sodium channels were partially purified and characterized. Multiple peaks of sodium channel phosphatase were detected after DEAE-Sephadex chromatography and gel filtration. All peaks were sensitive to a low concentration of okadaic acid (10 nM), which strongly suggests that phosphatase 2A is the major brain phosphatase dephosphorylating sodium channels. Individual fractions containing sodium channel phosphatase activity from both DEAE-Sephadex chromatography and gel filtration were subjected to immunoblot with anti-phosphatase 2Ac antibody. The results indicate that all fractions containing phosphatase activity also contained phosphatase 2Ac immunoreactivity. The fractions which stained most intensely in the immunoblots were the fractions containing the highest phosphatase activity in all cases. The molecular weights of the multiple sodium channel phosphatases estimated by gel filtration were 83 kDa, 147 kDa, and 141 kDa. These may represent isozymes of phosphatase 2A in brain.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
dc.subjectHealth Sciences, Toxicology.en_US
dc.subjectHealth Sciences, Pharmacology.en_US
dc.subjectChemistry, Biochemistry.en_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorRossie, Sandra S.en_US
dc.identifier.proquest1346421en_US
dc.identifier.bibrecord.b27226633en_US
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