Linked Life Data

12105958

Source:http://linkedlifedata.com/resource/pubmed/id/12105958

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2002-7-10
pubmed:abstractText
In heat denaturation studies conducted in the past the genetic variants of glycinin have been considered as a homogeneous group of proteins. In this work the validity of this assumption was tested. It was found by calorimetric studies that glycinin denatures heterogeneously at pH 7.6. When the temperature of isothermal treatment is increased from 70 to 82 degrees C the proportion of glycinin remaining native progressively decreases from 95% to 5% while the denaturation temperature of the glycinin remaining native increases from 88.5 to 95 degrees C. Similar trends were found for pH 3.8. Fractionation and subsequent analysis (MALDI-TOF and CE) of isothermally treated samples demonstrated that at pH 7.6 the heterogeneous denaturation is caused by differences in thermal stability of the genetic variants of glycinin. The stability increases in the order G2/G3/G1< A(4)< G5 < G4.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-8561
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4275-81
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Differences in denaturation of genetic variants of soy glycinin.
pubmed:affiliation
Center for Protein Technology TNO-WU, Wageningen, The Netherlands.
pubmed:publicationType
Journal Article, Comparative Study