The B-domain of recombinant human Factor VIII comprises 909 amino acids and is extensively N-and Oglycosylated, in that at least 20 different sites are occupied by numerous carbohydrate structures. This domain was incubated with trypsin and subjected to liquid chromatography electrospray ionization
Separation and characterization of the tryptic peptide mapping of recombinant bovine growth hormone by reversed-phase high-performance liquid chromatography electrospray mass spectrometry
โ Scribed by Jen P. Chang; Douglas E. Kiehl; Allison Kennington
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 144 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0951-4198
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โฆ Synopsis
Reversed phase high-performance liquid chromatography (RPHPLC) coupled with electrospray ionization mass spectrometry (ESI-MS) was used to separate and characterize the peptides resulting from the tryptic cleavage of somidobove, a recombinant bovine growth hormone. The tryptic digestion of somidobove was carried out at room temperature for 15 hours. The tryptic peptides were separated on a Zorbax SB300 C8 column with trifluoroacetic acid -acetonitrile gradient elution and characterized by LC/ESI-MS. Resulting single and combined peptide fragments were characterized by comparing the observed molecular mass with the calculated mass for these fragments.
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