Disease relevance of S-2302

• No activity was generated in prekallikrein-deficient plasma, and essentially normal levels (1.35 +/- 0.18 S-2302 U/ml) were measured in plasmas from three patients with factor XII deficiency [1].
• Generation of amidolytic activity towards the chromogenic substrate S-2302 after incubation with dextran sulphate (DXS), was found in ascites from patients with gastrointestinal cancer, but not in ascites from patients with benign liver disease [2].

High impact information on S-2302

• The Km and kcat values for the hydrolysis of H-D-Pro-Phe-Arg-p-nitroanilide by kallikrein or its light chain were identical [3].
• The kallikrein substrate H-D-Pro-Phe-Arg-p-nitroanilide was used in a direct spectrophotometric assay for activated Hageman factor (HF) [4].
• It showed kallikrein-like activity and hydrolyzed kallikrein substrates 2AcOH.H-D-Phe-Gly-Arg-pNA (CBS 33.27) and H-D-Pro-Phe-Arg-pNA (S-2302) [5].
• Following stimulation of lymphocytes in vitro, individual microwells were tested for growth by visual examination and for the TSP-1 protein/enzyme by analyzing cell lysates using either a specific rabbit anti-TSP-1 antiserum and/or the chromogenic model peptide substrate H-D-Pro-Phe-Arg-p-nitroanilide [6].
• Solutions of both plasmins undergo storage induced alteration, which is best recorded by Chromozym PL, whereas the other chromogenic substrates, S-2251 and S-2302, and casein are less sensitive, and the fibrin plate inadequate [7].

Biological context of S-2302

• Prekallikrein decreased significantly (p less than 0.01) from 1.49 +/- 0.15 S-2302 U/ml (mean +/- SEM) in early labor to 1.26 +/- 0.13 S-2302 U/ml in the immediate postpartum period [8].
• The medicinal leech salivary gland secretion deprived of hirudin antithrombin activity inhibits amidolytic (substrate S-2302) and kininogenase (substrate kininogen) activities of plasma kallikrein, the main component of the intrinsic mechanism of blood coagulation [9].

Anatomical context of S-2302

• The surface contacted plasmas cleaved the kallikrein-specific reagent S-2302 both after single surface contact, and after reincubation of surfaces in fresh plasma [10].

Associations of S-2302 with other chemical compounds

• It had no activity against elastin, fibrin, and the chromogenic substrates S-2805, S-2302 and S-2238 [11].
• The dextran sulfate-induced activation of prekallikrein at 0 degree C (assayed by its amidolytic activity on the chromogenic substate S-2302) could not be observed in either bovine or rabbit plasmas when compared to human plasma [12].
• In fractions from gel filtration of plasma acetone-activated in the presence of benzamidine (BPLa), kallikrein was assayed as S-2302 amidase, HK and LK were measured in rocket immunoassay, and HK and FXII were studied in PAGE immunoblot experiments [13].
• Jerdonase catalyzed the hydrolysis of BAEE, S-2238 and S-2302, which was inhibited by phenylmethylsulfonyl fluoride (PMSF), but not affected by ethylenediaminetetraacetic acid (EDTA) [14].
• Kallikrein activity was measured in urine, saliva and blood plasma samples from pregnant cows by using the chromogenic substrates S-2266 and S-2302 (Kabi, Sweden) [15].

Gene context of S-2302

• In contrast, the mean concentration in five plasma samples from patients deficient in HMW kininogen was 0.38 +/- 0.02 S-2302 U/ml [1].
• Kallikrein was assayed as plasminogen activator, S-2302 amidase and BAEe esterase [16].
• This peak coincided with alpha 2M (chromogenic and ELISA) and plasma kallikrein (S-2302), but FXII (measured with a substrate insensitive to kallikrein) eluted separately.(ABSTRACT TRUNCATED AT 250 WORDS)[17]
• Plasma prekallikrein was measured by the kallikrein-like activity on synthetic substrate S-2302 after activation of prekallikrein [18].
• Plasma prekallikrein was measured by its activity on substrate S-2302 after activation [19].

Analytical, diagnostic and therapeutic context of S-2302

• In fractions from gel filtration of CPLa kallikrein was assayed as S-2302 amidase, high molecular weight kininogen (HK) was measured in rocket immunoassays, and HK and FXII were studied in PAGE immunoblot experiments [20].
• Functional assays carried out with different peptide substrates (S-2222 for FXIIa, and S-2222, S-2302 and Bz-Pro-Phe-Arg-pNA for kallikrein) showed increases in OC plasma to about 150% for both proteases, in accordance with results obtained in radial immunodiffusion (RID) [21].

References