Linked Life Data

3100327

Source:http://linkedlifedata.com/resource/pubmed/id/3100327

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-2-20
pubmed:abstractText
Microcalorimetric titrations of the major isotype of parvalbumin (tPA) from toad (Bufo) skeletal muscle, with Ca2+ in the presence and absence of Mg2+ and with Mg2+ in the absence of Ca2+, have been carried out at 25 degrees C and pH 7.0. The results indicate that the two binding sites in each molecule are distinguishable from each other for both Ca2+ binding and Mg2+ binding. Such a characteristic is distinctly different from those of other parvalbumins. The enthalpy changes determined are distinctly different from those of bullfrog parvalbumins on Ca2+ or Mg2+ binding, but are similar to those on Mg2+-Ca2+ exchange. The results indicate that the reaction of Mg2+-Ca2+ exchange is driven almost entirely by the large favorable enthalpy change.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
209
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
77-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
A calorimetric study of Ca2+ binding by the parvalbumin of the toad (Bufo): distinguishable binding sites in the molecule.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't