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Monitoring of the Human Serum Albumin Carbonylation Level Through Determination of Guanidino Group Content.


Anal Biochem. 2012 Oct 24;


Authors: Aćimović JM, Jovanović VB, Srećković VD, Penezic Romanjuk AZ, Mandić LM


Abstract

Carbonylation of the protein amino, guanidine and thiol groups with α-oxoaldehydes (which are produced in higher quantities in diabetes, uremia, oxidative stress, aging and inflammation) is one of the important causes of vascular complications. For monitoring of the human serum albumin (HSA) carbonylation level a spectrophotometric method, based on the formation of colored adduct between guanidine group and thymol-sodium hypobromite reagent in the alkaline media was investigated. Beer's law is obeyed in the concentration range of Arg and protein guanidine groups from 1 to 40 mM. Precision of the method (RSD) was in the range of 0.9-2%. Accuracy was examined by standard addition method (recovery about 100%). The method was applied for monitoring of carbonylation level of HSA with methylglyoxal in vitro and of HSA isolated (using affinity chromatography) from sera of 21 patients with type 2 diabetes and 12 healthy persons. The content of guanidine groups in HSA isolated from diabetics (19.64±1.07 mM /mM albumin) was significantly lower (p <0.001) in comparison with a control group (21.87±1.02 mM/mM albumin). The method is simple and fast, it has good accuracy, precision and it is suitable for clinical practice, as well for in vitro protein carbonylation experiments.

PMID: 23103397 [PubMed - as supplied by publisher]