Procoagulant albumin (Pro-Alb) is an anionic form of albumin isolated
from normal human plasma that regulates vascular endothelial cell hemo
static properties, including induction of tissue factor activity. We i
nvestigated the biochemical modification of Pro-Alb that was associate
d with procoagulant - inducing activity. Tryptic digestion of Pro-Alb
identified greatest bioactivity in the carboxy-terminus of the molecul
e, a region associated with lipid binding sites. Activated charcoal tr
eatment and phopholipase C digestion reduced the procoagulant-inducing
activity of Pro-Alb, and Pro-Alb contained 2.3-fold more phosphorus t
han inactive albumin. We conclude that modification of albumin by phos
pholipid imparts tissue factor-inducing activity to Pro-Alb. (C) 1997
Elsevier Science Ltd.