thrombin cleavage site  (Thermo Fisher)

Journal: Science Advances

Article Title: Hemostatic B-knob–triggered microgels (BK-TriGs) to address bleeding in neonates

doi: 10.1126/sciadv.ady7698

Figure Lengend Snippet: ( A ) Schematic representation of the experimental timeline: neonatal fibrinogen injection, followed by microparticle injection, liver laceration, and subsequent blood loss monitoring over 10 min. ( B ) Time course of blood loss (grams of blood per gram of animal weight) in mice treated with saline or varying doses of BK-TriGs (10, 15, and 20 mg/kg), demonstrating dose-dependent hemostatic effects. ( C ) Total blood loss analysis showing significant reduction with BK-TriGs at 15 mg/kg compared to saline ( P < 0.001) and highlighting increased blood loss at 20 mg/kg ( P < 0.0001). ( D ) Comparative blood loss over time for mice treated with NB-ULCs, AK-ULCs, and BK-TriGs at 15 mg/kg, showing superior performance of BK-TriGs. ( E ) Total blood loss for the different particle treatments, indicating the significant efficacy of BK-TriGs ( P < 0.05) compared to other groups. Data are presented as the means ± SD.

Article Snippet: In each 50-μl reaction, 45.25 μl of plasma was mixed with 1 μl of Alexa Fluor 488–labeled human fibrinogen (10 μg/ml final; Thermo Fisher Scientific), 1.25 μl of CaCl 2 (200 mM stock; final 5 mM), and 2.5 μl of human thrombin (10 U/ml; Enzyme Research Laboratories, US) to initiate polymerization [thrombin (final 0.5 U/ml)].

Techniques: Injection, Saline

Journal: Gels

Article Title: Origin of the High Variability in Sol–Gel Phase Transitions: The Agar Gelation Model

doi: 10.3390/gels12040304

Figure Lengend Snippet: ( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human alpha thrombin at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.

Article Snippet: Human alpha thrombin was purchased by Enzyme Research Laboratories (South Bend, IN, USA).

Techniques: Derivative Assay, Enzymatic Assay