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           Search results for: Antibodies, Rabbit: Rabbit anti human Factor VII antiserum   

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Role of the COOH-terminal acidic region of A1 subunit in A2 subunit retention in human factor VIIIa.

Factor VIIIa is a heterotrimer of A1,A2 and A3-C1-C2 subunits which is labile due to a relatively weak affinity interaction between the A2 subunit and the Me(2+)-linked A1/A3-C1-C2 dimer. Previously we speculated that the acidic region at the COOH terminus of the A1 subunit was involved with the A2 subunit retention. This region, delineated by factor VIII residues 337-372, was chemically synthesized. Both the peptide, designated FVIII337-372, and an IgG fraction prepared from rabbit anti-FVIII337-372 antiserum inhibited the reconstitution of factor VIIIa from A1/A3-C1-C2 dimer plus A2 subunit. A primary component of the inhibitory activity of the peptide was attributed to its acidic nature based upon similar inhibition of factor VIIIa reconstitution using a synthetic polymer of aspartic acid. Trypsin cleaved the peptide at Arg359 and the resultant two fragments were isolated. Inhibitory activity was associated with the NH2-terminal fragment which contained 10 of the 13 acidic residues present in the original peptide. The fluorescence of a dansylated FVIII337-372 was enhanced 2-fold by A2 subunit and this effect was reversed by addition of excess unmodified peptide. The inhibitory activity of FVIII337-372 was attenuated by the presence of Ca2+. Ca2+ also inhibited the reconstitution of factor VIIIa in the absence of peptide and increased the rate and extent of factor VIIIa decay, suggesting that Ca2+ effectively shielded charges important for the intersubunit interactions. The above results support a role for this acidic region in the association of A2 subunit with A1/A3-C1-C2 dimer.

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Studies on immunological assay of vitamin K dependent factors. I. Measurement of factor VII antigen by radioimmunoassay.

A radioimmunoassay (RIA) for factor VII was developed using 125I-factor VII, anti-factor VII rabbit serum and anti-rabbit IgG goat serum. The lower limit of sensitivity in normal reference plasma was 3 X 10(-3) units/ml. Although the level of factor VII antigen (VII:Ag) in normal plasma samples (n = 20) 0.944 +/- 0.176 units/ml, correlated with that of factor VII coagulant activity (r = 0.89), VII:Ag level in paired normal sera showed a higher value (1.469 +/- 0.376 units/ml). The level of antigen according to RIA of factor VIIa activated by factor Xa increased 2.5-fold compared with that of unactivated factor VII. It is suggested that the polyclonal anti-factor VII produced in a rabbit had higher affinity for factor VIIa than for factor VII. In two out of seven patients with congenital factor VII deficiency, VII:Ag was detectable (0.04, 0.31 units/ml, respectively) whereas VII:C was less than 0.01 units/ml. In 12 warfarin-treated individuals, VII:C showed a lower level (0.121 +/- 0.063 units/ml) that that of VII:Ag (0.518 +/- 0.186 units/ml). During 4 weeks observation after stopping warfarin, VII:C and VII:Ag reached normal levels in 1 week. However, VII:C did not reach equivalence with VII:Ag until 4 weeks had elapsed.

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Fluid-phase immunoradiometric assay for the detection of qualitative abnormalities of factor VIII/von Willebrand factor in variants of von Willebrand's disease.

Antigenic reactivity of F.VIII/WF in variants of von Willebrand's disease (vWd) was studied with both fluid-phase and solid-phase immunoradiometric assays. Two different (rabbit and goat) 125I-labeled specific antibodies against purified F.VIII/WF were used in both their divalent (IgG) and their monovalent (Fab fragment) forms. Dose-response curves obtained by reacting a constant amount of antibody with serial dilutions of plasmas from normal or homozygous vWd demonstrated the specificity of the test. The accuracy was significantly higher with 125I-Fab fragments of goat anti-F.VIII/WF antiserum that intact goat IgG or rabbit IgG or Fab fragments. The significant decrease of the slope of the dose-response curves obtained with plasma from variants of vWd has been interpreted as due to the presence of abnormal F.VIII/WF molecules with decreased antigenic reactivity. A similar anomaly was found in cryosupernatant prepared from normal plasma, paralleling similarities demonstrated between variants of vWd and cryosupernatant. Results of experiments performed by reacting constant plasma dilutions from control or variants of confirmed the decreased antigenic reactivity of variant F.VIII/WF.

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Procoagulant and platelet aggregating properties of antilymphocyte sera.

Ten anti-human lymphocyte sera in clinical use at six transplant centers and five anti-nonhuman lymphocyte sera were studied for their procoagulant and platelet-aggregating properties. This investigation was initiated following the observation of a clinical episode of renal artery thrombosis, associated with the use of one of the sera in a patient who had received a cadaveric renal transplant. The procoagulant from this serum shortened the clotting times of individual samples deficient, respectively, in factors XII, XI IX, X VIII, and VII. Esterolytic activity, demonstrated on the substrate benzoylarginine ethyl ester, was completely inhibited by phenylmethylsulfonyl fluoride, but coagulant activity was variably affected. The platelet-aggregating activity (PAA) has been identified as a complement-fixing gamma G antibody that was absorbed from the antilymphocyte serum (ALS) with human spleen lymphocytes. Five of the ten anti-human lymphocyte sera showed varying procoagulant activity (PCA), and six sera demonstrated PAA. Three sera contained both activities. The presence of both PCA and PAA in the same preparation may predispose patients to thrombotic events, particularly if administered intravenously. Sera should be screened for PCA and PAA prior to clinical use, and sera with these properties should be used with caution.

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The effect of anti-rat clotting factor serum on the "prothrombin time".


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