Linked Life Data

5677

Source:http://linkedlifedata.com/resource/pubmed/id/5677

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9-10
pubmed:dateCreated
1976-8-2
pubmed:abstractText
The intereaction between proteins and acid polysaccharides is electrostatic in nature and leads to the formation of soluble charged and insoluble neutral complexes. The complex formation in the system casein-dextran sulphate is followed by means of turbidimetric titration. It depends on the pH value and the electrolyte concentration. On free electrophoresis, complexes formed below the isoelectric point of the protein exhibit anodic mobility, whereas pure casein migrates to the cathode. The protein in the complex is not able to bind amido black. Consequently, it cannot be detected electrophoretically by dyebinding. The results from viscosity and diffusion measurements are indicative of an increased hydrodynamic volume of the complexes.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0027-769X
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
929-33
pubmed:dateRevised
2009-11-11
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
[Interaction between proteins and acid polysaccharides].
pubmed:publicationType
Journal Article, English Abstract