Linked Life Data

7062252

Source:http://linkedlifedata.com/resource/pubmed/id/7062252

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-5-12
pubmed:abstractText
Human serum albumin was incubated at 37 degrees in 0.01 M phosphate buffer (pH 7.4) under sterile conditions for up to 10 days with labeled [14C]glucose (1-25 mg/ml). Glucose incorporated into albumin was calculated following extensive dialysis of the incubation mixture. The results indicated that glucose reacted with albumin by a nonenzymatic process involving Schiff base formation and Amadori rearrangement to a stable ketoamine derivative. The degree of glucosylation was dependent on the reaction time, glucose concentration, and pH. Glucosylation was enhanced when albumin was fatty acid free. Glucosylated albumin was separated from unmodified albumin by cation exchange chromatography on carboxymethylcellulose and quantitated colorimetrically with 2-thiobarbituric acid. Salicylate binding studies revealed that the glucosylated component had a decreased salicylate binding capacity accompanied by a reduction in the number of classes of binding sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-3549
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Glucosylated albumin and its influence on salicylate binding.
pubmed:publicationType
Journal Article, In Vitro