Protein co-isolated with human tissue factor impairs recovery of activity
SD Carson, SE Ross and RA Gramzinski
Department of Pathology, University of Colorado Health Sciences Center,
Denver 80262.
Preparations of human tissue factor isolated by immunoaffinity
chromatography contain variable amounts of 47,000 mol wt, 55,000 mol wt,
and multimeric tissue factor when analyzed without reduction on
polyacrylamide gels in sodium dodecyl sulfate (SDS). When analyzed after
reduction, the 47,000 mol wt tissue factor apoprotein and a protein of
about 12,000 mol wt are observed. Elution of tissue factor from
polyacrylamide gel slices, followed by reassociation with lipids, restored
proportionately much greater tissue factor activity with the 47,000-mol wt
protein than with the 55,000-mol wt form. Cyanogen bromide cleavage at the
single tissue factor methionine revealed that the 12,000-mol wt protein is
associated with the carboxyl-terminal peptide derived from the 47,000-mol
wt protein. These results reveal that association of the 12,000-mol wt
protein with the cytoplasmic domain of tissue factor can modulate its
activity in vitro.
Volume 71,
Issue 2,
pp. 520-523,
02/01/1988
Copyright © 1988 by The American Society of Hematology
