Linked Life Data

16592479

Source:http://linkedlifedata.com/resource/pubmed/id/16592479

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-6-29
pubmed:abstractText
The binding of the geometrical isomers (>/=99% pure) of juvenile hormone I to the hemolymph juvenile hormone binding protein of Manduca sexta (Lepidoptera, Sphingidae) was analyzed. A technique is described for isomer separation by micropreparative high-resolution liquid chromatography. Analysis of competition was performed by using a "batch adsorption" hydroxylapatite binding assay. Competition studies indicate that the naturally occurring isomer, 2E,6E,10cis, is bound with the highest affinity. Optimal binding appears to depend most heavily upon the configuration of the 2,3 double bond. Juvenile hormone binding protein shows a higher affinity for the 2E than for the 2Z configuration. The 6,7 double bond is of less importance in determining binding activity, and isomerism about the epoxide appears least important in conferring binding activity. The binding site may be a groove along the surface of the binding protein interacting with the side chains of juvenile hormone, including the ester methyl group. The grouping of the side chains and the ester methyl group thus constitutes a distinct hydrophobic face, and the hydrophobic interactions are essential in maintenance of the bound ligand.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Jan
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-9
pubmed:dateRevised
2010-9-14
pubmed:year
1978
pubmed:articleTitle
Specificity of the juvenile hormone binding protein: The geometrical isomers of juvenile hormone I.
pubmed:affiliation
Department of Biological Sciences, Northwestern University, Evanston, Illinois 60201.
pubmed:publicationType
Journal Article