フラグメントDのアミノ末端の構造を認識するモノクローナル抗体 (JIF-23) を用いたフィブリンのプラスミン分解産物の解析

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  • Analysis of Plasmin-digests of Cross-linked Fibrin Utilizing an Antibody Recognizing the Amino-Terminal Conformation of Fragment D

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Utilizing a monoclonal antibody, JIF-23, recognizing the disulf ided linked amino-terminal structure of the plasmic fragment D species of human fibrinogen, we analyzed the plasmic-digests of cross-linked (XL-) fibrin. By immunoblotting, JIF-23 was found to react with all species of the plasmic-digests of XL-fibrin, indicating that XL-fibrin was digested by plasmin in the same manner as fibrinogen and they had the same epitopes as fragment D species.<br>Utilizing JIF-23-coated latex beads, we established a rate-assay system sensitive solely to the digests possessing two epitopes as determined by aggregate formation by monitoring absorbance at 950 nm.<br>We selected the phase 3-digests of XL-fibrin described by C. W. Francis et al. as the standard material for calibration.<br>When the fibrin degradation products (XDP's) were separeted from plasmas of patients with DIC utilizing the antibody-conjugated Sepharose-4 B gels and analysed by SDS-PAGE, the arbitrary densitometric units were also well correlated with the measured D-dimer Values.<br>These data indicate that the XDP's in the DIC patient's plasmas were mainly the DD/E and DD/E-containing high molecular weight derivatives of XL-fibrin, apparently corresponding to the phase 3-digests of XL-fibrin.

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