Biochemical characterization of procoagulant albumin.
Procoagulant albumin (Pro-Alb) is an anionic form of albumin isolated from normal human plasma that regulates vascular endothelial cell hemostatic properties, including induction of tissue factor activity. We investigated the biochemical modification of Pro-Alb that was associated with procoagulant-inducing activity. Tryptic digestion of Pro-Alb identified greatest bioactivity in the carboxy-terminus of the molecule, a region associated with lipid binding sites. Activated charcoal treatment and phopholipase C digestion reduced the procoagulant-inducing activity of Pro-Alb, and Pro-Alb contained 2.3-fold more phosphorus than inactive albumin. We conclude that modification of albumin by phospholipid imparts tissue factor-inducing activity to Pro-Alb.
Liu
L
L
Department of Medicine, University of Utah Medical Center, Salt Lake City 84132, USA.
Murray
D K
DK
Dameron
C T
CT
Parker
C J
CJ
Rodgers
G M
GM
D000595:Amino Acid Sequence; D001777:Blood Coagulation; D001798:Blood Proteins / Q000737:chemistry; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D008969:Molecular Sequence Data; D012709:Serum Albumin / Q000737:chemistry*; D013925:Thromboplastin / Q000378:metabolism
D001798:Blood Proteins; D012709:Serum Albumin; D013925:Thromboplastin