Linked Life Data

12487438

Source:http://linkedlifedata.com/resource/pubmed/id/12487438

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2002-12-18
pubmed:abstractText
Surface plasmon resonance technique was investigated for the first time to study the apparent hydrophobicity and association properties of the major bovine caseins: alpha(s)-(alpha(s1)- and alpha(s2)-caseins in a 4:1 proportion), beta-, and kappa-caseins. The apparent hydrophobicities of the caseins were evaluated by a new method based on the binding level of casein on a hydrophobic sensor chip, and kinetic and equilibrium affinity constants were determined for the following casein interactions: alpha(s)/alpha(s), alpha(s)/beta, alpha(s)/kappa, beta/beta, and beta/kappa, using a sensor chip modified with covalent immobilized caseins. The study by surface plasmon resonance technology of these casein interactions under different conditions (pH, ionic strength, calcium concentration, chemical modification) demonstrated that, at neutral pH, electrostatic repulsive forces play an important role since an increase in ionic strength of the medium resulted in a stronger interaction. When charge repulsions were reduced by either acidification, increase in ionic strength, or dephosphorylation, casein interactions were reinforced, presumably due to weak attractive forces. Moreover, in this molecular model, we showed that addition of calcium greatly increased the binding response between the most phosphorylated caseins and that the added calcium (2 mM) participated directly in the formation of bridges between the phosphate groups of the casein molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-0302
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2711-21
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Casein interactions studied by the surface plasmon resonance technique.
pubmed:affiliation
Laboratoire de Génie Biologique et Sciences des Aliments, Université Montpellier II, 34095 Montpellier Cedex 5, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't