Literature DB >> 2777182

Radioimmunoassay for non-enzymatically glycated serum proteins.

M Kato1, H Nakayama, Z Makita, S Aoki, Y Kuroda, K Misawa, H Yoshida, K Yanagisawa, S Nakagawa.   

Abstract

We have developed a radioimmunoassay (RIA) for nonenzymatically glycated serum proteins. The polyclonal antibodies prepared against reduced glycated human albumin were specific for the glucitollysine residues of serum proteins. Serum proteins from diabetic patients (n = 25) contained 5.3 +/- 2.8 nmoles of glucitollysine/mg protein, compared to 2.0 +/- 0.2 in controls (n = 20). The intra- and inter-assay variables were 3.2-6.2% and 4.4-8.6%, respectively. Results from this assay procedure correlated well with those from the boronate affinity chromatography procedure (r = 0.94; P less than 0.001). The data suggested that diabetic serum proteins contained at least 2.5 times as much immunochemically detectable glucitollysine residures as normal serum proteins after reduction of the proteins with sodium borohydride.

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Year:  1989        PMID: 2777182     DOI: 10.1055/s-2007-1009204

Source DB:  PubMed          Journal:  Horm Metab Res        ISSN: 0018-5043            Impact factor:   2.936


  1 in total

1.  Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose.

Authors:  P J Thornalley; A Langborg; H S Minhas
Journal:  Biochem J       Date:  1999-11-15       Impact factor: 3.857

  1 in total

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