Linked Life Data

7460923

Source:http://linkedlifedata.com/resource/pubmed/id/7460923

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-4-21
pubmed:abstractText
Using negative staining and electron microscopic tilting techniques in conjunction with modelling experiments, the fine structure of chicken, sheep and rat pyruvate carboxylases has been studied. The overall configuration appears to be a tetrahedron-like structure consisting of two pairs of subunits in two different planes orthogonal to each other with the opposing pairs of subunits interacting with each other on their convex surfaces. The predominant form of the enzyme particles mounted and stained in the presence of acetyl-coenzyme A consisted of a compact, triangular outline enclosing three readily visible intensity maxima. When samples were mounted in the absence of acetyl-coenzyme A the molecules were more 'open' predominantly rhomboid structures. From tilting experiments it is concluded that the rhomboid images found in the absence of acetyl-coenzyme A represent partly or wholly flattened forms of the tetrahedron-like molecule. A feature of the enzyme when mounted in the absence of acetyl-coenzyme A was the existence of a 'cleft' along the longitudinal midline of each subunit, suggesting that the subunits may consist of two distinct domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
265-72
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Further electron microscope studies on pyruvate carboxylase.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't