| Mn2+-stimulated ATPase in rat brain. | |
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MedLine Citation:
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PMID: 6136925 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Divalent cation ATPases were prepared from rat brain synaptic vesicles, synaptosomal plasma membranes, and plasma membranes from the brain stem and sciatic nerve and tested for optimal stimulation by Mn2+, Mg2+, or Ca2+. ATPase in the synaptic vesicle subfraction was optimally stimulated by Mn2+. All plasma membrane preparations were optimally stimulated by Mg2+. Separate Mn2+ and Mg2+ ATPases could not be distinguished by either chemical inactivation or substrate preference criteria. Mn2+ stimulated ATPase in the micromolar range and it is suggested that Mn2+ interaction with ATPase may be of physiological and/or toxicological importance by being related to the cellular metabolism of this element. |
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Authors:
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J D Doherty; N Salem; C J Lauter; E G Trams |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Neurochemical research Volume: 8 ISSN: 0364-3190 ISO Abbreviation: Neurochem. Res. Publication Date: 1983 Apr |
Date Detail:
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Created Date: 1983-10-28 Completed Date: 1983-10-28 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 7613461 Medline TA: Neurochem Res Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 493-500 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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metabolism* Animals Brain / enzymology* Cations, Divalent Cell Membrane / enzymology Kinetics Male Rats Rats, Inbred Strains Sciatic Nerve / enzymology Synaptic Vesicles / enzymology* Synaptosomes / enzymology |
| Chemical | |
Reg. No./Substance:
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0/Cations, Divalent; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/manganese ATPase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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