Development and co-validation of porcine insulin certified reference material by high-performance liquid chromatography–isotope dilution mass spectrometry

Abstract

This article concerns the development and co-validation of a porcine insulin (pINS) certified reference material (CRM) produced by the National Institute of Metrology, People's Republic of China. Each CRM unit contained about 15 mg of purified solid pINS. The moisture content, amount of ignition residue, molecular mass, and purity of the pINS were measured. Both high-performance liquid chromatography-isotope dilution mass spectrometry and a purity deduction method were used to determine the mass fraction of the pINS. Fifteen units were selected to study the between-bottle homogeneity, and no inhomogeneity was observed. A stability study concluded that the CRM was stable for at least 12 months at -20 °C. The certified value of the CRM was (0.892 ± 0.036) g/g. A co-validation of the CRM was performed among Chinese, Japanese, and Korean laboratories under the framework of the Asian Collaboration on Reference Materials. The co-validation results agreed well with the certified value of the CRM. Consequently, the pINS CRM may be used as a calibration material or as a validation standard for pharmaceutical purposes to improve the quality of pharmaceutical products.

Establishment of measurement traceability for peptide and protein quantification through rigorous purity assessment—a review

“…Accurate protein purity can be obtained with the corrected mass fraction of the amino acids. This approach has been applied for the purity assessment of BSA [208] and pINS [209] and the results obtained agreed well with those by the mass balance approach.…”

“…The mass balance approach is usually used for the SI traceable value assignment of pure organic primary calibrators, but it has been extended to larger molecules recently. It has been successfully applied for purity assessment of peptides [26,53,103,106] and has been attempted for large proteins, notably to evaluate the purities of bovine serum albumin (BSA) [208] and porcine insulin (pINS) [209]. The purities of BSA and pINS were 0.962 g g −1 and 0.897 g g −1 by the mass balance approach.…”

“…The use of AAA based IDMS was demonstrated for quantification of proteins including bovine serum albumin (BSA) [208], C-Reactive Protein [19], porcine insulin [209], human erythropoietin [212], human serum albumin (HSA) [19,215], cystatine C (CysC) [19], human growth hormone [107], beta-2-microglobulin [19] and Ara h1 [19]. The expanded measurement uncertainty of IDMS AAA approaches was reported to be between 3% and 6%, with the largest contribution being the hydrolysis reproducibility [210].…”

Novel imidazolium-embedded N,N-dimethylaminopropyl-functionalized silica-based stationary phase for hydrophilic interaction/reversed-phase mixed-mode chromatography

“…As one of the most powerful separation techniques, highperformance liquid chromatography (HPLC) is widely used in many fields, such as food analysis and inspection, environmental analysis, pharmaceutical quality control, and biomolecule separation and detection [1][2][3][4][5][6][7]. Up until now, the most commonly used HPLC separation modes include reversedphase liquid chromatography (RPLC), hydrophilic interaction liquid chromatography (HILIC), normal-phase liquid chromatography (NPLC), ion-exchange chromatography (IEC), and size-exclusion chromatography (SEC).…”