The Formation and “Decay” of Xlla

Speer, R. J; Ridgway, Helen

doi:10.1055/s-0038-1655034

Cited by 4 publications

(4 citation statements)

References 4 publications

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“…The present results are also concordant with those of Speer and R id g w a y [23] who also found a decreasing activity of sodium stearate during incuba tion in plasma.…”

Section: Effect O F Ffa Salt On Blood Coagulationsupporting

confidence: 93%

Clot-Promoting and Platelet-Aggregating Effects of Fatty Acids

Prost-Dvojakovic¹,

Samama²

1973

Pathophysiol Haemos Thromb

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“…The present results are also concordant with those of Speer and R id g w a y [23] who also found a decreasing activity of sodium stearate during incuba tion in plasma.…”

Section: Effect O F Ffa Salt On Blood Coagulationsupporting

confidence: 93%

Clot-Promoting and Platelet-Aggregating Effects of Fatty Acids

Prost-Dvojakovic¹,

Samama²

1973

Pathophysiol Haemos Thromb

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“…In addition to the above inherent problems in the assay procedure, we were hampered in our efforts to establish the exact quantitative purification on a specific activity basis by the instability of the product after passage through DEAE cellulose column chromatography. The problem of decreasing activity with increasing purification due to conversion of active Hageman factor to its inactive form has been documented by many investigators (19,27,46,47,59,66). Because of t his we were forced to prove by exclusion that our final purified product was free from any other known coagulation factors and that at least qualitatively it had procoagulant activity in our assay systems.…”

Section: Discussionmentioning

confidence: 93%

“…At present, one cannot accurately state what happens between the time Hageman factor is activated and when factor Xa makes its appearance. It is because of t his, that different assay systems for Hageman factor have been reported (27,30,58,59,66). Furthermore, the assays are hampered by the inaccessability of true Hageman factor deficient human plasma, its instability and relative variation of factor XII content from one patient to another and the varying definitions of a Hageman factor unit.…”

Section: Discussionmentioning

confidence: 99%

Physico-Chemical and Immunological Properties of Bovine Hageman Factor

Gl¹,

As²,

Ef³

et al. 1971

Thromb Haemost

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SummaryBy using glass wool absorption followed by elution in strong salt solution and various precipitation methods and DEAE cellulose column chromatography, Hageman factor was purified from bovine plasma. Physico-chemical properties were studied in native protein and in 6 M urea (denatured) which was used in order to prevent monomer - polymer conversion. S°20,w was 7.07 in 0.1 M KC1 and 5.84 in 6 M urea. The intrinsic viscosity by Kragh’s method was 0.0540 ml/g inNaCl-phosphate buffer and 0.0815 ml/g in 6 M urea. Partial specific volume (v) by method based on amino acid residues in undenatured protein, was 0.724 cc/g. By using differential sedimentation equilibrium in 6 M urea-H20 and 6 M urea - D20 solution, v was determined as 0.740 cc/g. In urea, molecular weight (MW) was 142,000 as determined by meniscus depletion method. Similar values were obtained for nondenatured and denatured protein by Sephadex gel filtration, from amino acid composition using Brand’s method and Schachman’s equation. For undenatured and denatured Hageman factor, molar frictional ratios (f/fo) were 1.39 and 1.58, axial ratios were 5.0 and 7.0 and estimation of diffusion constant (D°20, w) based on S-rate, MW and v, gave values of 4.45 x 10-7 and 3.88 x 10-7 cm2/sec respectively. Our data indicate that the molecule was unfolded in 6 M urea solution. Two N-terminal groups, glycine and valine, were demonstrated by Edman procedure. Carbohydrate analysis revealed the following: hexosamine 0.8%, protein- bound hexose 1.9%, fucose 0.19% and sialic acid 0.35%. Isoelectric point was determined as 7.9 by electrofocussing technique. This protein migrated with gamma globulin on electrophoresis. Hageman factor was found to be a powerful immunogen. Anti Hageman factor reacted with both a plasma and a serum protein but not with purified IgG.

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“…5). Thus, rat anaphylaxis may serve as a suitable model for the investigation of the pathological regulation and interactions of factor Xlla-dependent pathways in in vivo conditions [26].…”

Section: Discussionmentioning

confidence: 99%

Activation and Consumption of Hageman Factor in the Anaphylactic Shock of the Rat

Fésüs¹,

Csaba²,

Muszbek³

1976

Int Arch Allergy Immunol

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In the early stages of anaphylactic shock of rats pretreated with Bordetella pertussis vaccine, a prompt and parallel activation of the factor XIIa-dependent intrinsic coagulation, kinin generation, and fibrinolytic acticity was observed. The coagulation studies, the similarity of anaphylactic results with those produced by a single injection of ellagic acid, and the effective inhibition of the anaphylactic and the ellagic acid-induced activation of these pathways by lysozyme all suggest that factor XII itself becomes activated in rat anaphylaxis. As the reaction proceeded, considerable anticoagulant activities emerged, but the bradykinin and the plasminogen activator levels even further increased. During the first 10 min of anaphylactic shock, factor XII was partly consumed and this was prevented by ε-aminocaproic acid infusion. The results show that in pathological conditions such as anaphylaxis there is an intimate in vivo interaction among the three factor Xlla-dependent pathways.

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The Formation and “Decay” of Xlla

Cited by 4 publications

References 4 publications

Clot-Promoting and Platelet-Aggregating Effects of Fatty Acids

Clot-Promoting and Platelet-Aggregating Effects of Fatty Acids

Physico-Chemical and Immunological Properties of Bovine Hageman Factor

Activation and Consumption of Hageman Factor in the Anaphylactic Shock of the Rat

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