Hydrostatic pressure effects on rabbit and echinoderm myosin ATPase
dc.contributor.author | Guthe, Karl F. | en_US |
dc.date.accessioned | 2006-04-17T15:19:32Z | |
dc.date.available | 2006-04-17T15:19:32Z | |
dc.date.issued | 1969-06 | en_US |
dc.identifier.citation | Guthe, Karl F. (1969/06)."Hydrostatic pressure effects on rabbit and echinoderm myosin ATPase." Archives of Biochemistry and Biophysics 132(1): 294-298. <http://hdl.handle.net/2027.42/32957> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DV06BT-P1/2/499e1b7f097fba3d769ed9d551a60f4f | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32957 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4240402&dopt=citation | en_US |
dc.description.abstract | When saturated with ATP, sea cucumber myosin hydrolyzes ATP about 15 times more slowly than rabbit myosin, as expected from the slower contraction time of the muscle. The Arrhenius plots coincide at low temperatures, but only the rabbit plot changes slope at higher temperatures. This unexpected change in slope apparently results from the use of veronal buffer. At high substrate concentrations in veronal buffer, the enzymatic activities of the two proteins depend identically on calcium ion and on pH. The two myosins are equally inhibited by pressure at low pH and activated at high, suggesting that structural features common to the two enzymes are responsible for pressure sensitivity and its pH dependence. | en_US |
dc.format.extent | 431872 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 | Hydrostatic pressure effects on rabbit and echinoderm myosin ATPase | 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 | Bermuda Biological Station, St. George's West, USA; Zoology Department, University of Michigan, Ann Arbor, Michigan1, USA. | en_US |
dc.identifier.pmid | 4240402 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32957/1/0000340.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(69)90365-8 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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