Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-3-25
pubmed:abstractText
Bovine beta-lactoglobulin is a globular whey protein that associates partly and reversibly in dimers in the native state. Static and dynamic light scattering techniques have been used to determine the relative amount of monomers and dimers, and to estimate their size and shape in different conditions. The effect of the ionic strength on the dimerisation has been studied at pH 2, where the protein is highly charged. A simple model, taking into account the monomer-dimer equilibrium and virial interactions has been used. The strength of the interactions depends on the amount of added salt, i.e. ionic strength, and influences the dimer dissociation. When the ionic strength decreases, the equilibrium is shifted towards the monomeric form. The dissociation, however, is only complete at very low concentration. The effect of temperature has been studied at pH 7 and low concentration where virial interactions are negligible. The dissociation increases with increasing temperature (5 degrees C - 76 degrees C). At high temperatures, protein-protein aggregation is fast, even at low concentration. The temperature dependence can be described using a simple Van't Hoff model, even at temperatures where aggregation occurs. The ionic strength and temperature dependence both indicate that beta-lactoglobulin solutions have to be considered as a mixture of monomers and dimers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0141-8130
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
213-21
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin.
pubmed:affiliation
Laboratoire de Chimie et Physico-Chimie Macromoléculaire, URA CNRS, Université du Maine, Le Mans, France.
pubmed:publicationType
Journal Article