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The N-terminal fragment of pro-B-type natriuretic peptide (NT-proBNP) is a useful biomarker for heart failure (HF) diagnosis. NT-proBNP is O-glycosylated within the central part and present in the circulation as a pool of molecules with different glycosylation levels. Currently, an automated NT-proBNP immunoassay that is manufactured by Roche is widely used for NT-proBNP measurements. This immunoassay is based on monoclonal antibodies (mAbs), one of which is specific to the partially glycosylated region of NT-proBNP (epitope 42-46 aar) and is known to detect only a sub-fraction of endogenous NT-proBNP. HyTest has designed an alternative type of immunoassay that utilizes two mAbs specific to non-glycosylated parts of the NT-proBNP molecule. It is currently unclear if epitope specificity of antibodies that recognize either partially glycosylated or non-glycosylated regions impacts the diagnostic value of NT-proBNP assays. THE AIM OF THIS STUDY was to compare the diagnostic accuracy of the glycosylation-dependent Roche NT-proBNP assay and the HyTest prototype NT-proBNP method that is based on mAbs that target glycosylation-free regions of NT-proBNP. PLASMA SAMPLES We used EDTA-plasma samples that were obtained from 51 patients. The current data suggests that NT-proBNP assays specific to non-glycosylated regions of NT-proBNP have at least the same clinical value for HF diagnosis as the Roche NT-proBNP assay specific only to a sub-fraction of endogenous NT-proBNP.We expect that a new generation of NT-proBNP assays that are not sensitive to the glycosylation of NT-proBNP will be introduced in the clinical practice.