Linked Life Data

427247

Source:http://linkedlifedata.com/resource/pubmed/id/427247

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-6-26
pubmed:abstractText
The fluorescence dye 1-anilino-naphthalene-8-sulphonic acid (ANS) was used as a probe of non-polar binding sites in the enzyme plasma amine oxidase. Steady fluorescence measurements indicate that ANS binds to a single binding site of the dimeric enzyme with a dissociation constant of 5 microns. This binding site is different from the catalytic binding site. Nanosecond emission anisotropy measurements were performed on the ANS-enzyme in an effort to detect independent rotation of the subunits in the native enzyme. The observed rotational correlation time (phi = 105 ns) corresponds to the rotation of a rigid dimeric macromolecule. A rotational correlation time of 120 ns was obtained with the enzyme labelled with pyrenebutyric acid. It is concluded that the dimeric enzyme does not exhibit any modes of flexibility due to independent rotation of the subunits in the nanosecond range.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-62
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Nanosecond spectroscopy of a dimeric enzyme: plasma amine oxidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.