Linked Life Data

8369288

Source:http://linkedlifedata.com/resource/pubmed/id/8369288

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1993-10-8
pubmed:abstractText
Human plasma lipoprotein[a] and autologous low-density lipoprotein were reacted with the fluorescent probe 6-acryloyl-2-(dimethylamino)naphthalene (acrylodan) previously reported to be specific for sulfhydryl groups. Reaction kinetics were biphasic in both cases. The reaction of bovine serum albumin with acrylodan was also biphasic. Monophasic kinetics were observed when protein free sulfhydryl groups were blocked by carboxamidomethylation prior to acrylodan reaction. A significant increase in total fluorescence was observed in the reaction of acrylodan with proteins containing no free sulfhydryl groups and with polylysine. The rates of these reactions were highly sensitive to pH. Fluorescence changes due to dissolution of probe into hydrophobic protein or lipid domains were minimal as was reaction of probe with phospholipid head groups. When isolated from acrylodan-labeled Lp[a], apo[a], which contains no free sulfhydryl groups, contained covalently bound acrylodan. These results suggest that acrylodan can modify the lysine residues of lipid-free proteins and may modify not only the free sulfhydryl groups of low-density lipoprotein and lipoprotein[a] but also reactive amino groups. We conclude that under these conditions, the use of this probe to quantify free sulfhydryl groups in these lipoproteins is infeasible.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9215-20
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Acrylodan can label amino as well as sulfhydryl groups: results with low-density lipoprotein, lipoprotein[a], and lipid-free proteins.
pubmed:affiliation
Department of Medicine, Baylor College of Medicine, Houston, Texas.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't