Lead ion activates phosphorylation of electroplax Na+- and K+- dependent adenosine triphosphatase [(NaK)-ATPase] in the absence of sodium ion
dc.contributor.author | Siegel, George J. | en_US |
dc.contributor.author | Fogt, Suzanne K. | en_US |
dc.date.accessioned | 2006-04-07T16:28:36Z | |
dc.date.available | 2006-04-07T16:28:36Z | |
dc.date.issued | 1976-06 | en_US |
dc.identifier.citation | Siegel, George J., Fogt, Suzanne K. (1976/06)."Lead ion activates phosphorylation of electroplax Na+- and K+- dependent adenosine triphosphatase [(NaK)-ATPase] in the absence of sodium ion." Archives of Biochemistry and Biophysics 174(2): 744-746. <http://hdl.handle.net/2027.42/21767> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DN44R9-NW/2/29079b1e75e45fd3924d8b7a3103fe6d | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/21767 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=132899&dopt=citation | en_US |
dc.description.abstract | PbCl2 in micromolar concentrations stimulates phosphorylation of electroplax microsomal protein in the absence of Na+. Other divalent cations showed little or no such effect. The (Mg2+ + Pb2+)- and (Mg2+ + Na+)-dependent membrane-bound protein kinase activities in electroplax particulate preparations exhibit properties in common, including their acid stability, ouabain sensitivity, ATP specificity, and molecular size. It is concluded that the (Mg2+ + Pb2+)-dependent phosphoprotein is part of the Na+-, K+-dependent adenosine triphosphatase [(NaK)ATPase]. The Pb2+-dependent product, in contrast to the Na+-dependent one, is insensitive to K+ and the hydrolysis of ATP is thus inhibited. | en_US |
dc.format.extent | 297771 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Lead ion activates phosphorylation of electroplax Na+- and K+- dependent adenosine triphosphatase [(NaK)-ATPase] in the absence of sodium ion | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Neurology Research Laboratory Neurology Department University of Michigan, Ann Arbor, Michigan 48104, U.S.A. | en_US |
dc.contributor.affiliationum | Neurology Research Laboratory Neurology Department University of Michigan, Ann Arbor, Michigan 48104, U.S.A. | en_US |
dc.identifier.pmid | 132899 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/21767/1/0000161.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(76)90405-7 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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