Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A).
The locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII were determined by sequence analysis of fragments produced by chemical and enzymatic digestions. The A1 and A2 domains of the heavy chain and the A3 domain of the light chain contain one free cysteine and two disulfide bonds, whereas the C1 and C2 domains of the light chain have one disulfide bond and no free cysteine. The positions of these disulfide bonds are conserved in factor V and ceruloplasmin except that the second disulfide bond in the A3 domain is missing in both factor V and ceruloplasmin. The positions of the three free cysteines of factor VIII are the same as three of the four cysteines present in ceruloplasmin. However, the positions of the free cysteines in factor VIII and ceruloplasmin are not conserved in factor V.
McMullen
B A
BA
Department of Biochemistry, University of Washington, Seattle 98195, USA.
Fujikawa
K
K
Davie
E W
EW
Hedner
U
U
Ezban
M
M
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D005169:Factor VIII / Q000737:chemistry*; D006801:Humans; D007460:Iodoacetamide; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011489:Protein Denaturation; D011994:Recombinant Proteins / Q000737:chemistry; D017421:Sequence Analysis
D004220:Disulfides; D010455:Peptides; D011994:Recombinant Proteins; D005169:Factor VIII; D003545:Cysteine; D007460:Iodoacetamide