scholarly journals Fibrinogen‐related protein, FGL2, of hamster cauda epididymal fluid: Purification, kinetic analysis of its prothrombinase activity, and its role in segregation of nonviable spermatozoa

2020 ◽  
Vol 87 (12) ◽  
pp. 1206-1218
Author(s):  
Subir K. Nagdas ◽  
Shamar Wallace ◽  
Don Eaford ◽  
Rashad Baker ◽  
Ky'ara Carr ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Related Protein ◽  
Epididymal Fluid ◽  
Prothrombinase Activity

scholarly journals Kinetic Analysis of a Unique Direct Prothrombinase,fgl2, and Identification of a Serine Residue Critical for the Prothrombinase Activity

2002 ◽  
Vol 168 (10) ◽  
pp. 5170-5177 ◽  
Author(s):  
Camie W. Y. Chan ◽  
Matthew W. C. Chan ◽  
Mingfeng Liu ◽  
Laisum Fung ◽  
Edward H. Cole ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Serine Residue ◽  
Prothrombinase Activity

Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis

2000 ◽  
Vol 85 (2-3) ◽  
pp. 169-177 ◽  
Author(s):  
Frank Wohnsland ◽  
Arndt A.P Schmitz ◽  
Michel O Steinmetz ◽  
Ueli Aebi ◽  
Guy Vergères
Keyword(s):  
Kinetic Analysis ◽  
Actin Polymerization ◽  
Related Protein

Myofibroblast-derived secreted frizzled-related protein 1 (SFRP1) can inhibit colorectal carcinoma field cancerization

2013 ◽  
Vol 51 (05) ◽  
Author(s):  
G Valcz ◽  
V Patai ◽  
I Füri ◽  
A Kalmár ◽  
B Péterfia ◽  
...  
Keyword(s):  
Colorectal Carcinoma ◽  
Field Cancerization ◽  
Related Protein

On the Natural Blood Coagulation Inhibitor System Investigations of Inhibitor Factors Based on Antithrombin Deficient Blood

1965 ◽  
Vol 14 (03/04) ◽  
pp. 473-489 ◽  
Author(s):  
O Egeberg
Keyword(s):  
Normal Level ◽  
Antithrombin Iii ◽  
Strong Support ◽  
Blood Protein ◽  
Coagulation Inhibitor ◽  
Inhibitor System ◽  
Normal Human ◽  
Partial Deficiency ◽  
Antithrombin Iii Activity ◽  
Prothrombinase Activity

SummaryNatural coagulation inhibitor factors were studied in sera, or in fractions of sera, from patients with congenital partial deficiency of antithrombin and from normal persons. In the patients’ sera the progressive antithrombin (antithrombin III) and heparin cofactor (antithrombin II) had both been measured around 50 per cent of normal level.No decreased activity could be demonstrated in the patients’ sera as to antiprothrombinase, the inhibitor against blood intrinsic prothrombinase activity.For anticonvertin, the inhibitor against the tissue convertin complex, the activity was found decreased to about the same level as that demonstrated for antithrombin III and II. The results lend strong support to the hypothesis that the activities measured as anticonvertin, antithrombin III and antithrombin II represent functions of the same blood protein, which on the other side appears to be distinct from antiprothrombinase. In accordance with this explanation, an antithrombin III concentrate had also antithrombin II and anticonvertin activity, and further, adsorption of a normal human serum with convertin appeared to specifically reduce its antithrombin III activity.The inhibitor against activated antihemophilic C factor (AHC’ = activated f. XI) was studied in sera adsorbed with BaS04 and celite. The inhibitor activity was found at normal level in the patients’ sera, consistent with the view that anti-AHC’ is distinct from antithrombin III, II and from anticonvertin. No acceleration of the anti-AHC’ activity could be demonstrated after addition to the inhibition mixture of weak solutions of heparin.The results are discussed.

Kinetic Aspects of the Interaction of Blood Clotting Enzymes

1965 ◽  
Vol 13 (01) ◽  
pp. 155-175 ◽  
Author(s):  
H. C Hemker ◽  
P.W Hemker ◽  
E. A Loeliger
Keyword(s):  
Kinetic Analysis ◽  
Enzyme Kinetics ◽  
Blood Clotting ◽  
Enzyme System ◽  
Enzyme Kinetic ◽  
Clotting Time ◽  
Standard Methods

SummaryApplication of the methods of enzyme-kinetic analysis to the results of clotting tests is feasible and can yield useful results. However, the standard methods of enzyme kinetics are not applicable without modifications imposed by the peculiarities of the blood-clotting enzyme system. The influence of the following complicating circumstances is calculated :1. Substrate is not present in excess.2. Only relative measures exist for concentrations of substrate or enzymes.3. Enzymes and substrates are often added together.4. Reagents are not pure.5. Clotting-time is our only measure for clotting-velocity.Formulas are deduced, which makes it possible to recognize the effect of these complications.

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