Production scale purification of biosynthetic human insulin by reversed-phase high-performance liquid chromatography

Kroeff, Eugene P.; Owens, Rebecca A.; Campbell, Emily L.; Johnson, R D; Marks, H I

doi:10.1016/s0021-9673(00)94274-2

Cited by 126 publications

(55 citation statements)

References 25 publications

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“…Because of the importance of insulin in animal metabolism, its chemical and structural properties have been extensively studied (Blundell et al, 1972;Chothia et al, 1983). Some chromatographic study of insulin has also Seen reported (Gross et al, 1988;Kroeff et al, 1989;McLeod et al, 1990), but little has been done to characterize the effect of metal coions on chromatographic behavior. This type of nonspecific aggregation will not be considered further in the current study and is mentioned here for its completeness.…”

Section: High Concentration Effectsmentioning

confidence: 99%

Effects of protein aggregation in isocratic nonlinear chromatography

et al. 1991

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Section: High Concentration Effectsmentioning

confidence: 99%

Effects of protein aggregation in isocratic nonlinear chromatography

et al. 1991

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“…The first approach involved the separate expression of each of the A-chain and B-chain followed by their purification and random oxidative combination [29]. This was followed by an improved process involving the expression of pro-insulin which is now the current method of choice for insulin production [30] as it entails just one sequence of fermentation and purification steps. Consequently, a similar method was also adapted developed for the expression of relaxin.…”

Section: Recombinant Dna Synthesis Of Relaxinmentioning

confidence: 99%

Synthetic relaxins

Hossain

Wade

2014

Current Opinion in Chemical Biology

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The relaxin subfamily of peptides within the human insulin superfamily consists of seven members including relaxin-2 and relaxin-3. The former is a pleiotropic hormone that is a vasodilator and cardiac stimulant in the cardiovascular system and an antifibrotic agent whereas the latter is primarily a neuropeptide involved in stress and metabolic control. Both possess the unique three-disulfide heterodimeric peptide structure of insulin. Consequently, the synthesis, both chemical and biological, of relaxin-2 and relaxin-3 has long represented a special challenge to further understanding their structural and functional relationships. This review highlights past and recent developments in the use of chemical and recombinant DNA methods of synthesis of these peptides and current resulting knowledge of their biology.

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“…Kroeff et al [115] reported a process for the purification of the biosynthetic human insulin (BHI) at the kilogram scale by a silica-based RPLC. The RPLC procedure was successfully integrated into the multimodal chromatographic production process used to purify large amounts of BHI.…”

Section: Reversed-phase Liquid Chromatographymentioning

confidence: 99%