Linked Life Data

3038019

Source:http://linkedlifedata.com/resource/pubmed/id/3038019

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-8-27
pubmed:abstractText
Thermal properties of bovine brain fodrin have been studied by circular dichroism and electron spin resonance and compared to those of bovine erythrocyte spectrin. Protein unfolding was induced either by urea or by a combination of heat and urea. The denaturation profiles of the two proteins, as measured by the changes in ellipticity at 222 nm as a function of temperature, were very similar but fodrin denaturation occurred at both higher temperatures and higher urea concentrations. In the absence of urea the thermal transition of spectrin was centered at 51 degrees C and that of fodrin at 54.5 degrees C. Proteins were also labeled with a maleimide analog spin probe. Spin-labeled fodrin showed a thermal transition similar to that of spectrin but centered at 46 degrees C instead of 42 degrees C. These findings indicated a close structural similarity of the two proteins but a slightly higher conformational stability of fodrin to both heat and urea.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
144-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Comparison of thermal properties of bovine spectrin and fodrin.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't