Chromozym t-PA

Chromozym t-PA (0.5 mM; 30 min) serves as a competitive chromogenic substrate for measuring the inhibition of TF-rFVIIa and TF-glycoPEGylated rFVIIa by AT/Heparin HY-17567, indicating that glycoPEGylation slightly reduces the rate of AT inhibition^[1].
Chromozym t-PA (1 mM) is hydrolyzed by fVIIa, GdVIIa, fVIIa·sTF, GdVIIa·sTF, fVIIa·TF/PCPS, and GdVIIa·TF/PCPS in amidolytic assays, with K_m values of 1.05-5.77 mM and k_cat values of 12.1-76.0 s^-1; its hydrolysis reports TF binding K_d values of 0.041 to 51.2 nM, Ca²⁺ half-maximal activation of < 20 to 520 μM, and EDTA-resistant sTF binding K_d,app of 1.7-3.2 μM^[2].
Chromozym t-PA (1 mM; 10 min at room temperature) monitors amidolytic activity in the purified factor VIIa binding assay; sTFAA-annV binds factor VIIa most strongly, with a K_d of 3.47 nM^[4].
Chromozym t-PA (150 µL; 37°C for 30 min) is used as a synthetic peptide substrate to measure t-PA hydrolysis activity; the reaction is terminated with citric acid, and absorbance is read at 405 nm^[5].
Chromozym t-PA (1 mM; 15-20 min) in the sTF1-219:FVIIa amidolytic assay: TF4A12 shows low (< 20%) amidolytic activity, and TF3H9 (2 μg/mL) neutralizes approximately 50% of FVII amidolytic activity^[8].
Chromozym t-PA (0.5-10 mM) hydrolysis is maintained in VIIaAla-40 but is significantly reduced by VIIaAla-99, with its K_m increasing to 1440 μM^[9].
Chromozym t-PA (0.5 mM) is hydrolyzed by TF1-218-VIIa and is not inhibited by XArg-15,Ala-195 or XGln-15,Ala-195, indicating no active-site competition for this small chromogenic substrate^[9].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.