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• W2399687576 abstract "Blood-clotting factors are generally assayed for their biological activity. The recent discovery, however, that some haemorrhagic conditions stem from the existence of structurally abnormal clotting factors rather than their deficiency or absence creates a need for additional assay methods. Thus abnormal forms offibrinogen (Blomback eta/., 1968) factor VIII (Denson et al., 1969), factor IX (Denson et al., 1968) and factor X (Denson et al., 1970) have been reported. If the structural abnormality is limited, as in the case of fibrinogen Detroit (Blomback et al., 1968), then abnormal factors could interact with antibodies raised against the corresponding normal molecule. Consequently, it appears desirable to assay clotting factors from patients with haemorrhagic disorders by radioimmunoassay as well as by conventional clotting tests. Radioimmunoassays for fibrinogen (Catt etal., 1968), prothrombin(Johnston etal., 1972) and theantihaemophilic factor, factor VIII (Hoyer, 1972) have been reported. The purpose of this present work was to develop a radioimmunoassay for factor X. Highly purified bovine factor X was prepared by the method of Esnouf et a]. (1 973). The chromatographic fraction, designated factor X, (Fujikawa et al., 1972) was used throughout this work. Factor X (20pg) was labelled with lz5I (1mCi) by using the chloramine-T method (Hunter & Greenwood, 1962) and also the method of enzymic iodination with lactoperoxidase (Holohan et al., 1973). In each case, the iodinated protein was purified by chromatography on DEAE-Sephadex. The former method led to 60% incorporation of the lZ5I into factor X by comparison with only 10% with the enzyme. Since both iodinated products were bound to the same extent (85%) by excess of antibody, the former method of iodination was used in this study. Rabbits were immunized against bovine factor X by multi-site subcutaneous injection. Immunoglobulins G, containing the resultant antibodies, were purified and coupled to Sepharose 4B as described by Murphy et al. (1973). The product is subsequently referred to as antibody-Sepharose conjugate, 1 mg of which was sufficient to bind 50 % of the amount (1.7ng) of labelled antigen used for radioimmunoassay. Radioimmunoassay mixtures comprised a suspension of antibody Sepharose conjugate (0.1 ml), labelled antigen (0.lml) in Michaelis buffer (Michaelis, 1931), pH7.3, diluted to lml with buffer. The buffer contained 1 % human serum albumin to minimize non-specific binding to the polypropylene assay tubes (capacity 2.5ml). The assay tubes were stoppered and rotated end over end throughout incubation for 20h at 5°C. Radioactivity bound to the antibody-Sepharose conjugate was counted after repeated centrifugation and washing with the above buffer containing 5 % Sepharose. The inert agarose particles facilitated retention of the conjugate during removal of the supernatant. Concentrations of factor X as low as 20ng/ml could be detected; the operative range, however, was 30-500ng/ml. No crossreactivity was observed with pure bovine prothrombin, thrombin or trypsin in concentrations up to lOOfig/ml. The immunoreactivity of factor Xa, however, was identical with that of factor X indicating that the immunogenic site for factor X did not reside in the activation peptide. The results further strengthen the evidence that factor Xa and thrombin are not both derived from the same molecule. Direct assay of fresh bovine plasma gave a concentration of factor X of 1 mg/100mI comparable with that reported by Esnouf et al. (1973)." @default.
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• W2399687576 date "1974-08-01" @default.
• W2399687576 modified "2023-09-27" @default.
• W2399687576 title "A Radioimmunoassay of Bovine Factor X" @default.
• W2399687576 doi "https://doi.org/10.1042/bst0020738" @default.
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