Linked Life Data

921939

Source:http://linkedlifedata.com/resource/pubmed/id/921939

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1978-1-27
pubmed:abstractText
Circular dichroic spectra in the visible wavelength region were used to investigate the local environment of Co(II), an activating metal, at the active site of rabbit muscle creatine kinase. There was a small spectral change when CoADP- was bound to creatine kinase, no change when creatine was added, and another small change when NO3- was added to form the transition state analogue. Using matrix rank analysis to quantitate these small spectral changes, a titratable group with a pK = 7.4 was found which modified the enzyme-bound metal-nucleotide interaction. These data suggest that, throughout the enzyme's catalysis, the metal-nucleotide interaction remains very similar in structure to the complex not bound to the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5364-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Circular dichroism of cobaltous complexes of creatine kinase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.