2010
DOI: 10.1373/clinchem.2010.148775
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Characterization of Molecular Forms of N-Terminal B-Type Natriuretic Peptide In Vitro

Abstract: BACKGROUND:The heterogeneity of circulating peptides may influence the interpretation of results from N-terminal profragment of BNP (NT-proBNP) assays. Our objective was to characterize the heterogeneity for better usability of the assays.

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Cited by 10 publications
(6 citation statements)
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“…NT-proBNP concentrations were determined by immunoassay specific to human NT-proBNP10–29 as previously reported [12,13]. NT-proBNP is a product of the same precursor and therefore reflects the secretion of the biologically active peptide BNP.…”
Section: Methodsmentioning
confidence: 99%
“…NT-proBNP concentrations were determined by immunoassay specific to human NT-proBNP10–29 as previously reported [12,13]. NT-proBNP is a product of the same precursor and therefore reflects the secretion of the biologically active peptide BNP.…”
Section: Methodsmentioning
confidence: 99%
“…It has subsequently been further characterised with many antisera in single and two-site immunoassays [80] and by MS after tryptic digestion [76]. This 76 amino acid peptide is produced from its precursor peptide proBNP…”
Section: Probnp and Nt-probnp Circulating Formsmentioning
confidence: 99%
“…With regard to oligomerization as the explanation for our results, we discussed various possibilities and found that oligomerization, which is not our original idea (3 ), appeared to be the one most consistent with our results (4 ). We are open to other explanations.…”
Section: In Replymentioning
confidence: 48%