Enhanced secretory ability for the human factor VIII light chain produced in baculovirus-infected insect cells.
The light and truncated heavy chains of human factor VIII, expressed separately in baculovirus-infected insect cells, exhibited different secretory behaviour when compared with each other and with a biologically active fusion molecule of the truncated heavy and light chains. The light chain was very efficiently secreted into culture medium, as judged by high extracellular protein levels and the absence of evidence for light chain retention within cells. Alternatively, proteins containing the heavy chain sequence were poorly secreted and appeared to be sequestered within cells, suggesting that regions within the heavy chain are responsible for the low levels of secreted protein which have generally been observed for recombinant factor VIII.
Webb
E
E
Research and Development Division, CLS Limited, Parkville, Victoria, Australia.
Tkalcevic
J
J
Edwards
S
S
Hocking
D
D
Nisbet
I
I
D000818:Animals; D016367:Baculoviridae; D001483:Base Sequence; D005169:Factor VIII / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D015870:Gene Expression / Q000502:physiology; D006801:Humans; D015151:Immunoblotting; D007124:Immunoenzyme Techniques; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018411:Spodoptera / Q000166:cytology / Q000821:virology*
D011994:Recombinant Proteins; D005169:Factor VIII