Linked Life Data

33975

Source:http://linkedlifedata.com/resource/pubmed/id/33975

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-5-26
pubmed:abstractText
Pellicles were isolated from Paramecium caudatum for a study of the properties of its insoluble ATPase [EC 3.6.1.3] activity. Pellicular ATPase was solubilized by sonication and fractionated by sucrose density gradient centrifugation. The sedimentation coefficient of the ATPase was about 9S. The ATPase required Ca2+ for maximum activation. Addition of neutral salts to the assay medium inhibited the activity. Substrate specificity for ATP was low; other nucleoside triphosphates were hydrolyzed at about the same rate as ATP; AMP, pyrophosphate, and p-nitrophenyl phosphate were not hydrolyzed. The ATPase activity of the pellicle preparation had a pH optimum at pH 6.5, and a Michaelis constant of 9 micrometer. On the other hand, the enzymatic properties of the ATPase were somewhat modified by the procedure of solubilization and fractionation. The pellicular ATPase does not resemble ciliary dynein ATPase or the soluble ATPase of Tetrahymena.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
367-73
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Calcium-activated adenosine triphosphatase activity of pellicles from Paramecium caudatum.
pubmed:publicationType
Journal Article