Linked Life Data

7460899

Source:http://linkedlifedata.com/resource/pubmed/id/7460899

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-4-13
pubmed:abstractText
The phosphoserine present in troponin T of freshly isolated skeletal muscle troponin P1-TI2C was dephosphorylated by alkaline phosphatase and the resulting troponin TI2C characterized by phosphorous content and gel electrophoresis in presence of sodium dodecylsulfate. Both complexes bind Ca2+ in an identical manner with a K0.5 of 5.3 X 10(-9) M for the Ca2+/Mg2+ binding sites and of 1.1 X 10(-6) M for the Ca2+-specific sites. 3.5 mM Mg2+ lowers the K0.5 value at the Ca2+/Mg2+ binding sites of 1.3 X 10(-7) M in the phospho-troponin P1-TI2C and leaves nearly unchanged the value of the dephosphorylated troponin TI2C at 1.2 X 10(-8) M. At 10 mM Mg2+ only one dissociation constant of about 1.0 X 10(-6) M is determined with both complexes. In analogy dephosphorylation of troponin P1-TI2C reduces the affinity for Mg2+ at the Ca2+/Mg2+ binding sites from 6.7 X 10(-5) M to 2.0 X 10(-3) M. Again the Mg2+-specific sites are uninfluenced. The possibility is discussed that removal of the phosphate group from troponin T allows the interaction of the N-terminal domain of troponin T with other amino acid side chains of troponin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
325-32
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Comparison of the Mg2+ and Ca2+ binding properties of troponin complexes P1-TI2C and TI2C.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't