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human α-thrombin  (Prolytix)

 
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    Prolytix human α-thrombin
    Human α Thrombin, supplied by Prolytix, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+%CE%B1-thrombin/human+%CE%B1+thrombin/pmc11909436__BLOODA_ADV___2024___013810___mmc1-1-39-44
    Average 90 stars, based on 1 article reviews
    human α-thrombin - by Bioz Stars, 2026-09
    90/100 stars

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    Synthesized:

    Article Title: Investigating Protein-Nucleic Acid Binding Interactions with Diethylpyrocarbonate Covalent Labeling-Mass Spectrometry.
    Article Snippet: Nucleic acids are important biomolecules that facilitate numerous cellular functions and have in recent years become promising candidates for treating disease.. Consequently, there is a need for methods to characterize protein interactions with these molecules.. Here, we demonstrate that diethylpyrocarbonate (DEPC) covalent labeling−mass spectrometry (CL-MS) can provide structural information for protein-nucleic acid binding by characterizing the binding sites of two DNA aptamers specific to thrombin.

    Article Title: Deep Association between Transglutaminase 1 and Tissue Eosinophil Infiltration Leading to Nasal Polyp Formation and/or Maintenance with Fibrin Polymerization in Chronic Rhinosinusitis with Nasal Polyps
    Article Snippet: A solution containing 1.75 mg/mL fibrinogen (061-03691)/(Wako Pure Chemical Co., Tokyo, Japan) and 0.5, 1, 2, 4 μg/mL factor XIIIA (HCXIIIA-0165)/(Prolytix, Essex Junction, VT, USA) or 0.5, 1, 2, 4 μg/mL TGM 1 (T009)/(Zedira Gmbh, Darmstadt, Germany) in a 50 mM Tris HCl buffer of pH 7.4 containing 10 mM CaCl 2 was incubated and then clotted in the presence and absence of 1.25 μg/mL human α-thrombin (Prolytix, Essex Junction, VT, USA).

    Article Title: Platelets and MMP?9 contribute to esophageal cancer invasion via CD40?CD154 interactions
    Article Snippet: Platelets were activated by pre-warming at 37°C for 5 min, followed by the addition of 1 U human α-thrombin (Prolytix).

    Article Title: Bait and Cleave: Exosite-Binding Peptides on Quantum Dots Selectively Accelerate Protease Activity for Sensing with Enhanced Sensitivity.
    Article Snippet: Human α-thrombin, factor Xa, and plasmin were from Prolytix (Essex Junction, VT) and were received as solutions in 50% v/v glycerol/water.

    Article Title: Nuclease-assisted selection of slow-off rate aptamers
    Article Snippet: Human α-thrombin and human factor Xa were purchased from Prolytix.

    Article Title:
    Article Snippet: Platelet agonists included: a thrombin receptor activating peptide (T6, SFLLRN) synthetized by the Rockefeller University Proteomics Resource Center; collagen type I from equine tendons tail purchased from Chrono-Log Corp (Havertown, PA); ristocetin obtained from Sigma-Aldrich; von Willebrand factor and human α-thrombin (Thr) purchased from Prolytix (Essex Junction, VT).

    Article Title: Bait and Cleave: Exosite-Binding Peptides on Quantum Dots Selectively Accelerate Protease Activity for Sensing with Enhanced Sensitivity.
    Article Snippet: The advantageous optical properties of quantum dots (QDs) motivate their use in a wide variety of applications related to imaging and bioanalysis, including the detection of proteases and their activity.. Recent studies have shown that surface chemistry on QDs is able to modulate protease activity, but only nonspecifically.. Here, we present a strategy to selectively accelerate the activity of a particular target protease by as much as two orders of magnitude.

    Labeling:

    Article Title: Investigating Protein-Nucleic Acid Binding Interactions with Diethylpyrocarbonate Covalent Labeling-Mass Spectrometry.
    Article Snippet: Nucleic acids are important biomolecules that facilitate numerous cellular functions and have in recent years become promising candidates for treating disease.. Consequently, there is a need for methods to characterize protein interactions with these molecules.. Here, we demonstrate that diethylpyrocarbonate (DEPC) covalent labeling−mass spectrometry (CL-MS) can provide structural information for protein-nucleic acid binding by characterizing the binding sites of two DNA aptamers specific to thrombin.

    Article Title: Deep Association between Transglutaminase 1 and Tissue Eosinophil Infiltration Leading to Nasal Polyp Formation and/or Maintenance with Fibrin Polymerization in Chronic Rhinosinusitis with Nasal Polyps
    Article Snippet: A solution containing 1.75 mg/mL fibrinogen (061-03691)/(Wako Pure Chemical Co., Tokyo, Japan) and 0.5, 1, 2, 4 μg/mL factor XIIIA (HCXIIIA-0165)/(Prolytix, Essex Junction, VT, USA) or 0.5, 1, 2, 4 μg/mL TGM 1 (T009)/(Zedira Gmbh, Darmstadt, Germany) in a 50 mM Tris HCl buffer of pH 7.4 containing 10 mM CaCl 2 was incubated and then clotted in the presence and absence of 1.25 μg/mL human α-thrombin (Prolytix, Essex Junction, VT, USA).

    Article Title: Platelets and MMP?9 contribute to esophageal cancer invasion via CD40?CD154 interactions
    Article Snippet: Platelets were activated by pre-warming at 37°C for 5 min, followed by the addition of 1 U human α-thrombin (Prolytix).

    Article Title: Bait and Cleave: Exosite-Binding Peptides on Quantum Dots Selectively Accelerate Protease Activity for Sensing with Enhanced Sensitivity.
    Article Snippet: Human α-thrombin, factor Xa, and plasmin were from Prolytix (Essex Junction, VT) and were received as solutions in 50% v/v glycerol/water.

    Article Title: Nuclease-assisted selection of slow-off rate aptamers
    Article Snippet: Human α-thrombin and human factor Xa were purchased from Prolytix.

    Article Title:
    Article Snippet: Platelet agonists included: a thrombin receptor activating peptide (T6, SFLLRN) synthetized by the Rockefeller University Proteomics Resource Center; collagen type I from equine tendons tail purchased from Chrono-Log Corp (Havertown, PA); ristocetin obtained from Sigma-Aldrich; von Willebrand factor and human α-thrombin (Thr) purchased from Prolytix (Essex Junction, VT).

    Article Title: Bait and Cleave: Exosite-Binding Peptides on Quantum Dots Selectively Accelerate Protease Activity for Sensing with Enhanced Sensitivity.
    Article Snippet: The advantageous optical properties of quantum dots (QDs) motivate their use in a wide variety of applications related to imaging and bioanalysis, including the detection of proteases and their activity.. Recent studies have shown that surface chemistry on QDs is able to modulate protease activity, but only nonspecifically.. Here, we present a strategy to selectively accelerate the activity of a particular target protease by as much as two orders of magnitude.



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    ( 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 <t>alpha</t> <t>thrombin</t> 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.
    Human Alpha Thrombin, supplied by Enzyme Research Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+%CE%B1-thrombin/human+thrombin+%CE%B1/pmc13116384-152-0-6
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    human α thrombin native protein  (Thermo Fisher)
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    ( 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 <t>alpha</t> <t>thrombin</t> 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.
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    human α thrombin  (Sysmex Corporation)
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    ( 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 <t>alpha</t> <t>thrombin</t> 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.
    Human α Thrombin, supplied by Sysmex Corporation, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human α thrombin  (Yeasen Biotechnology)
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    ( 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 <t>alpha</t> <t>thrombin</t> 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.
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    Average 86 stars, based on 1 article reviews
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    human α-thrombin  (Prolytix)
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    ( 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 <t>alpha</t> <t>thrombin</t> 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.
    Human α Thrombin, supplied by Prolytix, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+%CE%B1-thrombin/human+%CE%B1+thrombin/pmc11909436__BLOODA_ADV___2024___013810___mmc1-1-39-44
    Average 90 stars, based on 1 article reviews
    human α-thrombin - by Bioz Stars, 2026-09
    90/100 stars
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    enzyme human α-thrombin  (Biopharm GmbH)
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    ( 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 <t>alpha</t> <t>thrombin</t> 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.
    Enzyme Human α Thrombin, supplied by Biopharm GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+%CE%B1-thrombin/bovine+thrombin/us12351648-2087-12-15
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    human α thrombin  (Thermo Fisher)
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    Thermo Fisher human α thrombin
    ( 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 <t>alpha</t> <t>thrombin</t> 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.
    Human α Thrombin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human α thrombin - by Bioz Stars, 2026-09
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    human α-thrombin ht 1002a  (Enzyme Research Laboratories)
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    Enzyme Research Laboratories human α-thrombin ht 1002a
    ( 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 <t>alpha</t> <t>thrombin</t> 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.
    Human α Thrombin Ht 1002a, supplied by Enzyme Research Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+%CE%B1-thrombin/human+%CE%B1+thrombin+ht+1002a/pm40499720-58-0-6
    Average 90 stars, based on 1 article reviews
    human α-thrombin ht 1002a - by Bioz Stars, 2026-09
    90/100 stars
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    Image Search Results


    ( 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.

    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