Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-4-8
pubmed:abstractText
The binding to human serum albumin of three cephalosporins of pharmacological interest: cefoperazone, ceftriaxone and cefsulodin was studied by ultrafiltration and differential scanning calorimetry methods. The identification of the binding sites in albumin was also performed using probes for the so-called sites I, II, bilirubin and fatty acids binding sites. Albumin showed two types of binding sites for cefoperazone and ceftriaxone, while for cefsulodin it showed a single type of binding site. The affinity values were: 5.6 10(4) M-1 and 3.1 10(4) M-1 for cefoperazone and ceftriaxone respectively, while cefsulodin showed low affinity (3.8 10(2) M-1). It was found that only cefoperazone interacted in a slight way with site I on serum albumin, while site II and the bilirubin binding site have capacity of binding the three cephalosporins assayed. Ceftriaxone and cefoperazone showed capacity to bind to the fatty acids binding site on albumin. These cephalosporins increased the thermal stability of the protein, suggesting that these ligands are favouring the compact structure of the native form of the protein more than the unfolded form.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
823-31
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
A comparative study of the binding characteristics of ceftriaxone, cefoperazone and cefsulodin to human serum albumin.
pubmed:affiliation
Departamento de Química-Física, Facultad de Ciencias Bioquímicas y Farmacéuticas, CIUNR and CONICET, Universidad Nacional de Rosario, Argentina.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't