Linked Life Data

2526696

Source:http://linkedlifedata.com/resource/pubmed/id/2526696

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-8-31
pubmed:abstractText
The actin dependence of the rate and magnitude of the initial phosphate burst was measured using both quench-flow and stopped-flow kinetic techniques. These studies revealed that even at high actin concentrations the magnitude of the phosphate burst was a significant fraction of the magnitude that exists in the absence of actin. Furthermore, it was shown that the rate of the burst rises rapidly as a function of the actin concentration. Detailed modeling with the four-state model revealed that if the predicted Vmax is constrained to be approximately equal to the extrapolated value (double reciprocal plot) and if the apparent dissociation constant of subfragment-1 to actin divided by the apparent activation constant of the actin-activated myosin ATPase activity (Kbinding/KATPase) is constrained to be considerably different from one, then the model is unable to simultaneously account for the ATPase activity and the rate and magnitude of the initial inorganic phosphate burst.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0009-7330
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
515-25
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Biochemical kinetics of porcine cardiac subfragment-1. II. Pre-steady-state studies of the initial phosphate burst.
pubmed:affiliation
Department of Medicine, State University of New York, Stony Brook 11794.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't