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PMID: 6221022 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Identity and Origin of the ATPase activity associated with neuronal microtubules. I. The ATPase activity is associated with membrane vesicles.

The Journal of cell biology ·Vol. 96 ·No. 5 ·1983-05-00 ·Pages 1298-305

Murphy DB, Hiebsch RR, Wallis KT

Abstract

Microtubule protein purified from brain tissue by cycles of in vitro assembly-disassembly contains ATPase activity that has been postulated to be associated with microtubule-associated proteins (MAPs) and therefore significant for studies of microtubule-dependent motility. In this paper we demonstrate that greater than 90% of the ATPase activity is particulate in nature and may be derived from contaminating membrane vesicles. We also show that the MAPs (MAP-1, MAP-2, and tau factors) and other high molecular weight polypeptides do not contain significant amounts of ATPase activity. These findings do not support the concept of "brain dynein" or of MAPs with ATPase activity.

MeSH Terms
Adenosine Triphosphatases/metabolism Animals Centrifugation, Density Gradient Chromatography, Gel Dyneins/analysis Male Microscopy, Electron Microtubule-Associated Proteins Microtubules/enzymology Neurons/enzymology Proteins/metabolism Swine
Chemicals
Microtubule-Associated Proteins Proteins Adenosine Triphosphatases Dyneins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Murphy D B
Hiebsch R R
Wallis K T
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34 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1983-05-00
Pages
1298-305
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2112664
Subset
IM
Grants
NCI NIH HHS · CA 00645 · United States
NIGMS NIH HHS · GM 26155 · United States
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