Phospholipid binding properties of human placental anticoagulant protein-I, a member of the lipocortin family
JF Tait, D Gibson, K Fujikawa - Journal of Biological Chemistry, 1989 - ASBMB
Human placental anticoagulant protein-I (PAP-I) is a member of the lipocortin/calpactin/
annexin family of Ca 2+-dependent phospholipid binding proteins. PAP-I was labeled with
fluorescein 5-isothiocyanate (1 mol/mol); this derivative had anticoagulant activity identical
to the unlabeled protein and could be used to measure Ca 2+-dependent binding to
phospholipid vesicles through changes in fluorescence quenching. At 1.2 mM Ca 2+, 0.50 M
ionic strength, pH 7.4, 25° C, fluorescein-labeled PAP-I bound to phospholipid vesicles …
annexin family of Ca 2+-dependent phospholipid binding proteins. PAP-I was labeled with
fluorescein 5-isothiocyanate (1 mol/mol); this derivative had anticoagulant activity identical
to the unlabeled protein and could be used to measure Ca 2+-dependent binding to
phospholipid vesicles through changes in fluorescence quenching. At 1.2 mM Ca 2+, 0.50 M
ionic strength, pH 7.4, 25° C, fluorescein-labeled PAP-I bound to phospholipid vesicles …