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Human α-thrombin was selectively and irreversibly inactivated with mCP(PBA)-F (pseudo first order rate constant k1=3.7x10-3 sec-1 23°). The initial velocities of inactivation followed simple enzyme-substrate kinetics (Km(app)=72.7 μM, k2=3x10-3 sec-1). mCP(PBA)-F was determined to be an affinity labeling reagent for both α and β/γ-thrombins (7% α, 20% β and 78% γ) as (1)[3H]mCP(PBA)-F was stochiometrically incorporated (1.07 mole/mole for α thrombin and 1.19 mole/mole for β/γ-thrombin), (2) [14C]iPr2P-F inactivated α and β/γ-thrombin did not react with mCP(PBA)-F, and (3) the analog o-(2-chloro-5-sulfonylf luorophenylureido)phenoxy benzene lacking the benzamidine, only caused 14% inactivation of α-thrombin. [14C]iPr2P-F was only found on the B chain (Mr 32,000) but [3H]m(PBA)-F label was distributed 20% on the A chain and 80% on the B chain in reduced and alkylated α-thrombin electrophoresed in 10% PAGE-SDS-6 M urea. The labeling pattern of β/γ-thrombin with [14C]iPr2-F and [3H]mCP(PBA)-F revealed that 14C label was on the B chain active site fragments of β-thrombin (Mr ≈ 23,000) and γ-thrombin (Mr ≈ 12,000), but the 3H label was on 20% the A chain and 80% on fragments of Mr 6000-10,000. The results suggest that mCP(PBA)-F reacts with residues exclusive of the active site serine within ~ 10 Å radius of the anionic binding site.(Supported by NIH Grants AI 11231, AM 17351, CA 17376, HL 13160 and HL 18825)

thrombosis and haemostasis

Exo-Site Affinity Labeling of Human α(CLOTTING) and β/γ(NONCLOTTING) m[o-2-CHLORO-5-Sulfonylfluorophenylureido) Phenoxybutoxy] Benzamidine (mCP(PBA)-F)