Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis

✍ Scribed by Joanne C. Severs; Mechelle Carnine; Hugo Eguizabal; Kuldip K. Mock

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 128 KB
• Volume: 13
• Category: Article
• ISSN: 0951-4198
• DOI: 10.1002/(sici)1097-0231(19990615)13:11<1016::aid-rcm599>3.0.co;2-5

✦ Synopsis

Recombinant Factor VIII (rFVIII) is involved in the cascade of biochemical reactions leading to blood coagulation and is used for the treatment of haemophilia A. Plasma-derived FVIII (pdFVIII) has been reported to be post-translationally modified by sulfation of tyrosine residues at positions 346, 1664, 1680, 718, 719 and 723. 1 This report describes the quantitation of tyrosine sulfate residues in BHK-derived, human rFVIII by amino acid composition analysis and the identification of their positions in the polypeptide sequence using a combination of liquid chromatography and electrospray ionization mass spectrometry in the analysis of proteolytic digests of the protein.