Linked Life Data

9187248

Source:http://linkedlifedata.com/resource/pubmed/id/9187248

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-7-1
pubmed:abstractText
Incubation of dimeric MM-creatine kinase (MM-CK) with high NaCl or LiCl concentrations results in dissociation of the subunits and complete enzyme inactivation. In NaCl, this process, which depends on protein concentration, may be described according to a two-state model where the dimer can be reversibly converted into compact folded monomers (D <--> 2M). At LiCl concentrations higher than 2-2.5 M, MM-CK is recovered in two monomeric states: an inactive compact species (M) and a more expanded form (EF), which represents 15-20% of the population. Thus, in LiCl, a three-state model (D <--> 2M --> 2EF) more adequately accounts for our experimental results. The monomeric species (M) obtained in NaCl and LiCl exhibits some properties of the molten globule state described in guanidine hydrochloride. Indeed, this form is compact and devoid of any enzymatic activity; it maintains a high degree of secondary structure and binds 8-anilino-1-naphthalenesulfonate. The formation of this intermediate induces the exposure of a second tryptophan (among the four present) which is located at the monomer-monomer interface in the native structure. In LiCl, the monomeric species (M) is irreversibly converted into a less compact form (EF) which seems to have lost a large part of its secondary structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
1339
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
277-88
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
High salt concentrations induce dissociation of dimeric rabbit muscle creatine kinase. Physico-chemical characterization of the monomeric species.
pubmed:affiliation
UPRESA 5013 CNRS-Lyon I, Biomembranes et Enzymes Associés, Villeurbanne, France.
pubmed:publicationType
Journal Article