Linked Life Data

20301118

Source:http://linkedlifedata.com/resource/pubmed/id/20301118

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2010-8-23
pubmed:abstractText
The suppression of the thermal aggregation of glycogen phosphorylase b (Phb) from rabbit skeletal muscle by the chaperonin GroEL is studied using dynamic light scattering. It is shown that the decrease in the rate of Phb aggregation under the action of GroEL is due to the transition of the aggregation process from the kinetic regime, wherein the rate of aggregation is limited by diffusion of the interacting particles, to a regime where the sticking probability for the colliding particles becomes lower than one (reaction-limited cluster-cluster aggregation). The analytical-ultracentrifugation data show that elevated temperatures induce dissociation of the dimeric Phb. The formation of a complex between the denatured monomeric form of Phb and the dissociated forms of GroEL is detected during heating at 46 degrees C.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1616-5195
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
768-74
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Effect of GroEL on thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle.
pubmed:affiliation
Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky 33, Moscow, Russia. eronina@inbi.ras.ru
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't