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- W2040374384 abstract "To help ensure reliability of proinsulin measurements and define the optimal matrix for conducting routine bioanalysis of this prognostic biomarker, we undertook a systematic evaluation of its in vitro stability. For this study, we subjected mono-radioiodinated forms of hPI and its cleaved metabolites to size-exclusion chromatography (FPLC™-SEC employing a Superdex-75 10/30 HR column) to characterize their elution profiles following incubation in human serum and plasma. We determined that intact hPI is a substrate for serine-like protease(s) that are present in human serum. Furthermore, RIA analysis of the elution profile of unlabeled peptide demonstrated that the B–C junction is cleaved preferentially. Thus, in vitro degradation of hPI represents a potential pathway for the formation of cleaved metabolites. Our findings confirmed that EDTA plasma is the preferred matrix for quantitative determination of intact hPI and its cleaved metabolites. We concluded the SEC strategy employed in this study is broadly applicable to evaluating the in vitro stability of other peptides/proteins of diagnostic or therapeutic interest." @default.
- W2040374384 created "2016-06-24" @default.
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- W2040374384 date "2009-03-01" @default.
- W2040374384 modified "2023-09-26" @default.
- W2040374384 title "Application of size-exclusion chromatography in the investigation of the in vitro stability of proinsulin and its cleaved metabolites in human serum and plasma" @default.
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- W2040374384 doi "https://doi.org/10.1016/j.jchromb.2009.01.035" @default.
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