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Results for “FACTOR XII”

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PubMed1965

Activated human Hageman factor (XII).

An improved method for the isolation of highly purified active human Hageman factor has been described. An overall recovery of 25% with a purification of 10(6) has been achieved. Certain of the physical and chemical characteristics of XII have been elucidated. Selective chemical modification of functional groups and a variety of enzymatic assays have been employed in an effort to shed light on the mechanism of action of this procoagulant.

Amino Acids↗
PubMed1975

A new family with congenital factor XII deficiency.

The case of a patient with Hageman trait and his family study are reported. Commercial plasma thromboplastin time (PTT) reagents showed a good sensitivity for detecting the plasma defect. By prolonging the incubation time of the mixture containing PTT reagent and factor XII-deficient plasma the abnormal coagulation times were not corrected. Thus, a concomitant Fletcher factor deficiency could be excluded.

Blood Coagulation Disorders↗
PubMed1990

The Arthus reaction in cats deficient in Hageman factor (factor XII).

A study was made of the Arthus reaction in an animal model of Hageman-factor deficiency, namely Hageman trait cats, and in control cats with normal Hageman-factor activity. At three time points, there was a significant decrease (P less than 0.01) in the size of the cutaneous Arthus reaction to chicken red blood cells in biopsies from Hageman trait cats compared with the reaction in biopsies from control animals. Injection of a positive control, histamine, and a negative control, phosphate-buffered saline, produced no significant differences between the two groups. Hageman trait cats had a significant decrease (P less than 0.001) in the number of neutrophils in the skin lesions compared with controls. When Hageman trait cats were injected intravenously with purified cat Hageman factor, Arthus reactions were similar to those observed in control cats.

Animals↗
PubMed1988

Inositolphospholipid-accelerated activation of prekallikrein by activated factor XII and its inhibition by beta 2-glycoprotein I.

Inositolphospholipid-accelerated activation of prekallikrein by alpha-factor XIIa was determined by measuring the appearance of kallikrein amidolytic activity towards the chromogenic substrate, D-prolyl-phenylalanyl-arginyl p-nitroanilide (S-2302). The activation reaction did not exhibit normal Michaelis-Menten kinetics. The Hill coefficient was found to be 1.6 indicating that the activation followed an allosteric reaction mechanism. The temperature dependence of the reaction showed a thermal transition at 30 degrees C, which in addition to the allosteric reaction mechanism is indicative of a conformational change of prekallikrein following binding to the inositolphospholipid. The reaction exhibited pH optimum at pH 7.2 and ionic strength optimum at 50 mM NaCl. At optimal conditions the apparent KA value and the kcat/KA value for factor XIIa on prekallikrein were calculated to be 73 nM and 9.3 x 10(6) s-1 M-1, respectively. Kinetic constants could not be calculated at salt concentrations higher than the optimal concentrations, as Lineweaver-Burk plots were curvilinear in agreement with the Hill coefficient greater than unity. The activation was inhibited competitively by beta 2-glycoprotein I with a Ki value of 77 nM as determined by the Dixon plot.

Drug Synergism↗