Linked Life Data

21312376

Source:http://linkedlifedata.com/resource/pubmed/id/21312376

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-2-11
pubmed:abstractText
The use of many plasma expanders (PEs) is often limited by undesirable side effects, such as red blood cell (RBC) aggregation (hydroxyethyl starch), nephrotoxicity (dextran), and extravasation (albumin). Despite its natural prevalence in the bloodstream, human serum albumin (HSA) can increase the risk of mortality when administered to patients with increased vascular permeability (i.e., patients suffering from burns, septic shock, and endothelial dysfunction). The harmful extravasation of HSA can be limited by polymerizing HSA to increase its molecular size. In this study, HSA was nonspecifically cross-linked with glutaraldehyde at different cross-link densities by varying the molar ratio of glutaraldehyde to HSA. The results of this study show that the weight-averaged molecular weight (MW), viscosity, and extent of RBC aggregation of polymerized HSA increases with increasing cross-link density, whereas the colloid osmotic pressure (COP) decreases with increasing cross-link density. Interestingly, circular dichroism measurements indicate that the secondary structure of HSA is unaffected by polymerization. Altogether, these results show that glutaraldehyde can effectively cross-link HSA to produce high MW polymers, yielding a novel series of potential PEs that exhibit low COP and high viscosity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1520-6033
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 American Institute of Chemical Engineers (AIChE).
pubmed:issnType
Electronic
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
290-6
pubmed:dateRevised
2011-7-27
pubmed:meshHeading
pubmed:articleTitle
Synthesis and biophysical properties of polymerized human serum albumin.
pubmed:affiliation
William G. Lowrie Dept. of Chemical and Biomolecular Engineering, The Ohio State University, Columbus, OH 43210, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural