Linked Life Data

6789754

Source:http://linkedlifedata.com/resource/pubmed/id/6789754

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1981-9-25
pubmed:abstractText
Both immobilization techniques described in this work seem appropriate for this allosteric enzyme. However, the kinetic behavior of the dCMP deaminase trapped in a protein membrane is markedly different from that observed with the enzyme in solution and with the enzyme gelled on an artificial membrane. The enzyme, in fact, in all instances loses its cooperative action toward the substrate and even the allosteric ligands, or they do not affect the activity, or it behaves in a completely different way. In particular, dTTP seems to behave as a noncompetitive inhibitor. These effects can be attributed either to the freezing of the enzyme in one of its conformations or, more generally, to the effect of physical constraints and diffusional resistances. Further studies are in progress to distinguish between the contributions of each one of these phenomena to the kinetic behavior of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:volume
369
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Characterization and control of an immobilized allosteric enzyme system.
pubmed:publicationType
Journal Article