Linked Life Data

340937

Source:http://linkedlifedata.com/resource/pubmed/id/340937

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1978-3-10
pubmed:abstractText
Recent advances in the studies of the aggregation of G-actin monomers, containing one molecule of ATP, to long filaments of F-actin, with a concomitant hydrolysis of the nucleotide to ADP, are reviewed. With the aid of omega-ATP, the association and dissociation rate constant of the nucleotide could be determined. The binding of the nucleotide is enhanced by the binding of one Ca++ ion, probably at a different site. The delta G value of the Mg++ or Ca++ induced polymerization has been determined to --39 to--59 kJ/mole, the critical protein concentration for the ATP-G-actin to ADP-F-actin conversion is very strongly influenced by the concentration of bivalent cations. The rate constants of the protein monomers, and the rate and equilibrium constants for the propagation step show the process to be extremely cooperative. Actin shows the interesting phenomenon of translocational head-to-tail polymerization, which may be regulated by ATP. The contact sites between the monomers in F-actin have been labeled by chemical modification. Two tryosine residues, 53 and 69, are probably close to one of the two sites. The ATP binding sites has been labeled by an ATP analog, and there is evidence that it is close to the contact site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3-13
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
The polymerization reaction of muscle actin.
pubmed:publicationType
Journal Article, Review