Characterization of bovine factor XIIa (activated Hageman factor)

Biochemistry ◽  
1977 ◽  
Vol 16 (19) ◽  
pp. 4182-4188 ◽  
Author(s):  
Kazuo Fujikawa ◽  
Kotoku Kurachi ◽  
Earl W. Davie
Keyword(s):  
Hageman Factor ◽  
Factor Xiia ◽  
Bovine Factor

Activation of bovine factor VII (proconvertin) by factor XIIa (activated Hageman factor)

Biochemistry ◽  
1977 ◽  
Vol 16 (19) ◽  
pp. 4189-4194 ◽  
Author(s):  
Walter Kisiel ◽  
Kazuo Fujikawa ◽  
Earl W. Davie
Keyword(s):  
Factor Vii ◽  
Hageman Factor ◽  
Factor Xiia ◽  
Bovine Factor

Isolation and characterization of bovine factor XII (Hageman factor)

Biochemistry ◽  
1977 ◽  
Vol 16 (10) ◽  
pp. 2270-2278 ◽  
Author(s):  
Kazuo Fujikawa ◽  
Kenneth A. Walsh ◽  
Earl W. Davie
Keyword(s):  
Factor Xii ◽  
Hageman Factor ◽  
Isolation And Characterization ◽  
Bovine Factor

INTERACTIONS OF DYSFUNCTIONAL Cl-INHIBITORS FROM PATIENTS WITH TYPE II HEREDITARY ANGIONEUROTIC EDEMA (HANE) WITH ACTIVATED HAGEMAN FACTOR (FACTOR XIIa).

1987 ◽  
Author(s):  
V H Donaldson ◽  
M D B H Mitchell
Keyword(s):  
Normal Serum ◽  
Type Ii ◽  
Inhibitor Protein ◽  
Amidolytic Activity ◽  
Hageman Factor ◽  
Hereditary Angioneurotic Edema ◽  
Coagulant Activity ◽  
Antigenic Properties ◽  
Factor Xiia

Type II HANE is characterized by a deficiency of Cl-inhibitor (Cl-INH) activity in serum which is associated with a dysfunctional inhibitor protein having a normal or increased quantity o|_the antigenic properties of normal serum Cl-inhibitor. Dysfunctional Cl-INH proteins were purified from members_of eight different kindred with Type II HANE and compared to normal Cl-inhibitor with respect to their inhibitory activity directed against the amidolytic and clot-promoting properties of purified activated Hageman factor. All but one dysfunctional Cl-inhibitor blocked the amidolytic activity of ellagic acid-activated Hageman factor; all eight blocked the clot-promoting activity of Hageman factor activated in solutions of sulfatides and BSA. The inhibition _of amidolytic activity was equal to or greater than that of normal Cl-INH (Donaldson, et al., 3. Clin. Invest. 75:124,1985). The impairment of the specific Hageman factor coagulant activity of activated Hageman factor by six^f the eight dysfunctional inhibitors was less than that of the normal Cl-inhibitor, although readily measured. Dysfunctional Cl-inhibitor proteins were also heterogeneous with respect to their formation of stable complexes and their susceptibility to cleavage by Hageman factor activated with BSA-sulfatides when analyzed in SDS-gel electrophoresis. Although these observatons cannot be directly applied to in vivo pathophysiologic changes in plasma, dysfunctional Cl-inhibitors do have the potential of regulating activated Hageman factor.

scholarly journals Cabbage seed protease inhibitor: a slow, tight-binding inhibitor of trypsin with activity toward thrombin, activated Stuart factor (factor Xa), activated Hageman factor (factor XIIa), and plasmin

Blood ◽  
1990 ◽  
Vol 75 (1) ◽  
pp. 108-115 ◽  
Author(s):  
TH Carter ◽  
BA Everson ◽  
OD Ratnoff
Keyword(s):  
Tight Binding ◽  
Factor Xa ◽  
Clot Formation ◽  
Dot Blot ◽  
Induce Platelet Aggregation ◽  
Hageman Factor ◽  
Blot Technique ◽  
Binding Inhibition ◽  
Factor Xiia ◽  
Cabbage Seed

Abstract An inhibitor of procoagulant and fibrinolytic enzymes was derived from cabbage seeds by a procedure using acetone precipitation, ion-exchange chromatography, and gel filtration. The cabbage seed inhibitor was a 10- Kd monomeric protein with intrachain disulfide bonds. This preparation prevented clot formation in whole blood and blocked the ability of thrombin to induce clot formation in plasma and to induce platelet aggregation. A number of proteases were inhibited, as demonstrated by using purified enzymes in amidolytic assays. Tight-binding inhibition was observed for activated Stuart factor (factor Xa) and plasmin. Inhibition of thrombin and activated Hageman factor (factor XIIa) was observed with a molar excess of inhibitor. No inhibition was detected for activated plasma thromboplastin antecedent (factor XIa), plasma kallikrein, or C1 esterase. Reaction progress curves for trypsin indicated slow, tight-binding inhibition, with an apparent inhibition constant in the nanomolar range or less. The electrophoretic mobility of trypsin was altered by the inhibitor in nondenaturing polyacrylamide gel electrophoresis (PAGE) but not in sodium dodecyl sulfate (SDS)- PAGE, indicating noncovalent bonding. Only partial reversal of trypsin inhibition could be demonstrated by washing the inhibitor from enzyme immobilized on solid beads. A dot-blot technique with cabbage seed inhibitor was capable of detecting 10 ng nitrocellulose-bound trypsin. The dot-blot technique also appeared capable of detecting plasmin. These findings demonstrated the potential utility of this inhibitor as a probe for detection of tightly bound proteases. In summary, cabbage seed extracts contain an inhibitor with activity toward a broad range of proteases important to hemostasis. To our knowledge, this agent represents the first inhibitor isolated from a plant source that inhibits thrombin.

scholarly journals Production and characterization of a murine monoclonal antibody against a heavy chain of Hageman factor (factor XII)

Blood ◽  
1985 ◽  
Vol 65 (5) ◽  
pp. 1263-1268 ◽  
Author(s):  
H Saito ◽  
T Ishihara ◽  
H Suzuki ◽  
T Watanabe
Keyword(s):  
Monoclonal Antibody ◽  
Heavy Chain ◽  
Procoagulant Activity ◽  
Factor Xii ◽  
Contact Activation ◽  
Hageman Factor ◽  
Heavy Chains ◽  
Charged Surfaces ◽  
Normal Human

Abstract A murine hybridoma cell line that produces a monoclonal antibody to human Hageman factor (HF, factor XII) is described. The antibody (P 5–2– 1) consists of mouse IgG2b heavy chains and lambda light chains, selectively neutralizes HF procoagulant activity, and prevents the proteolytic cleavage of HF during contact activation in plasma. When HF is exposed to P 5–2–1 before the absorption of HF to kaolin, HF procoagulant activity is markedly inhibited. In contrast, P 5–2–1 does not interfere with HF activity after the adsorption of HF to kaolin. P 5–2–1 does not inactivate the prekallikrein–activating activity of 28,000–mol wt HF fragments (HFf). P 5–2–1 binds exclusively to the 40,000mol wt portion of a heavy chain of HF and inhibits the adsorption of HF to negatively charged surfaces. P 5–2–1 immobilized on Sepharose can be used to deplete HF from normal human plasma. This immunoaffinity-depleted plasma is indistinguishable from congenital HF- deficient plasma and can be used as the substrate for HF procoagulant activity assay.

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