Literature DB >> 10368977

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

J C Severs1, M Carnine, H Eguizabal, K K Mock.   

Abstract

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. 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.

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Year:  1999        PMID： 10368977     DOI： 10.1002/(SICI)1097-0231(19990615)13:11<1016::AID-RCM599>3.0.CO;2-5

Source DB:  PubMed          Journal:  Rapid Commun Mass Spectrom        ISSN： 0951-4198            Impact factor:   2.419


  6 in total

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4.  Structural investigation of zymogenic and activated forms of human blood coagulation factor VIII: a computational molecular dynamics study.

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Journal:  BMC Struct Biol       Date:  2010-02-25

5.  Acidic residues C-terminal to the A2 domain facilitate thrombin-catalyzed activation of factor VIII.

Authors:  Jennifer L Newell; Philip J Fay
Journal:  Biochemistry       Date:  2008-07-22       Impact factor: 3.162

6.  Taking down the FLAG! How insect cell expression challenges an established tag-system.

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  6 in total

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