High impact information on Ile-pro-arg-p-NA

• The k(cat)/K(m) value for hydrolysis of the chromogenic peptidyl substrate S-2288 by VIIa-30 (103 mm(-)1s(-)1) was 3-fold higher than that of wild-type VIIa (30.3 mm(-)1 s(-)1) in the presence of soluble tissue factor (sTF) [1].
• In the presence of recombinant TF and 5 mM Ca2+, the peptide inhibited the amidolytic activity of rVIIa toward the synthetic substrate, S-2288 [2].
• In addition, like the intact Fn, both the 10-kDa fragment and the synthetic peptide could remarkably enhance the amidolytic activity of t-PA in a dose-dependent manner, as shown by using S-2288 as a chromogenic substrate [3].
• The light chain was fully active on the tripeptide substrate H-D-isoleucyl-L-prolyl-L-arginine p-nitroanilide (S-2288) and partially active on plasminogen [4].
• Poly-Arg and poly-Lys showed predominantly competitive inhibition kinetics, although decreases in the k(cat) values for the chromogenic substrate S-2288 were also observed [5].

Associations of Ile-pro-arg-p-NA with other chemical compounds

• The purified plasminogen activator cleaved S-228 to a greater extent than S-2444, although UK cleaved S-2444 to a greater extent that S-2288 [6].

Gene context of Ile-pro-arg-p-NA

• In contrast, when the amounts of enzyme used were standardized on the basis of absorbance generated in a direct assay employing the chromogenic substrate S-2288 and then titrated with PAI-1, these differences in susceptibility to inhibition were not observed [7].
• The kinetic analyses of the hydrolysis of S-2288 by t-PA showed increase in kcat from 5.17/sec to 7.75/sec in the presence of 75 micrograms/ml of C9-5 without change in Km [8].
• A highly purified preparation of human plasma factor VIIa was submitted to chromogenic assays with S-2288 factors IXa, Xa, activated protein C and thrombin being absent [9].

Analytical, diagnostic and therapeutic context of Ile-pro-arg-p-NA

• A two-stage chromogenic assay monitoring S-2288 hydrolysis showed that PB readily blocked mTF-dependent or rbTF-dependent FVII activation, which was verified by the diminished activated factor VII (FVIIa) formation derived from the proteolytic cleavage of its zymogen factor VII on Western blotting analyses [10].
• Solutions of IV-1 paste prepared under different conditions were assayed for evidence of protease activity by Western blots of alpha(1)-PI following SDS-PAGE, by azocaseinolytic and amidolytic (S-2288) assays, and by zymography, and for the extent of alpha(1)-PI oligomerization by Western blots following nondenaturing PAGE [11].

References