Characterization of intact and trypsin-digested biosynthetic human growth hormone by high-pressure liquid chromatography☆
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Cited by (57)
The proteomics of N-terminal methionine cleavage
2006, Molecular and Cellular ProteomicsCitation Excerpt :If the protein has an N terminus associated with a risk of non-processing, various methods may be used to prevent Met retention: (i) adjusting expression conditions to optimize MAP activity according to the rate of protein synthesis in vivo (58), (ii) in vitro processing with purified wild-type or engineered MAP (59–62), (iii) dual co-overproduction of MAP and the protein of interest in vivo (25, 63, 64), (iv) processing in vitro or in vivo of the N terminus with another amino- or endoprotease (65–67), or (v) fusion of the ORF to a propeptide or ubiquitin sequence and use of endogenous signal peptidase specificity (68, 69). This last strategy has also proved successful for residues that cannot be unmasked by NME (this study, Fig. 3), such as the thrombin inhibitor hirudin, which must have Ile at its N terminus for biological activity, or human growth hormone, which must have Phe at its N terminus (70–73). In Archaea, most mature proteins have Ala, Met, Gly, Ser, Thr, or Pro at their N terminus (10).
Eliminating disulfide exchange during glutamyl endopeptidase digestion of native protein
1999, Journal of Chromatography ARapid verification of disulfide linkages in recombinant human growth hormone by tandem column tryptic mapping
1998, Journal of Chromatography APreventing the generation of artifacts during peptide map analysis of recombinant human insulin-like growth factor-I
1996, Analytical Biochemistry
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An abstract of these results was presented at the International Symposium on High-Pressure Liquid Chromatography of Proteins and Peptides, held in Washington, D. C., on November 16–17, 1981.