Linked Life Data

8519760

Source:http://linkedlifedata.com/resource/pubmed/id/8519760

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
1996-1-25
pubmed:abstractText
The slowly hydrolyzed ATP analog adenosine 5'-(gamma-thiotriphosphate) (ATP gamma S) has been used in many studies of the muscle motor protein myosin in order to form a stable "weak binding" state analogous to the actin-S1-ATP complex However, the results from studies using ATP gamma S do not always agree with the results of experiments using ATP. The binding of myosin subfragment-1-ATP gamma S to actin has now been studied in some detail to determine its relationship to the actin-S1-ATP state. The binding of myosin subfragment-1-ATP gamma S to actin-troponin-tropomyosin is similar in affinity to the binding of myosin subfragment-1-ATP. Like myosin subfragment-1-ATP, the binding is not Ca(2+)-dependent, and most importantly, myosin subfragment-1-ATP gamma S does not stabilize the active configuration of actin-troponin-tropomyosin. Thus, myosin subfragment-1-ATP gamma S is an analog of myosin subfragment-1-ATP but must be used with caution for two reasons: (1) The binding of ATP gamma S to regulated actomyosin subfragment-1 is Ca(2+)-sensitive, and errors can be made in the interpretation of results if proteins are not fully saturated with nucleotide and a mixture of weak and strong binding states is present. (2) At the high concentrations of myosin subfragment-1 used in some experiments, significant amounts of ADP may form.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16039-45
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Adenosine 5'-(gamma-thiotriphosphate): an ATP analog that should be used with caution in muscle contraction studies.
pubmed:affiliation
East Carolina University School of Medicine, Greenville, North Carolina 27858-4354, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.