AI Article Synopsis
- The study assessed the effectiveness of a radiolabeled F(ab')2 fragment of the T2G1s monoclonal antibody in detecting thrombus (blood clots) using gamma camera imaging, confirming a high level of immunoreactivity post-labeling.
- Different molar ratios for 111In labeling were tested, revealing that overall immunoreactivity (81%-89%) remained stable despite variations.
- Binding analysis indicated that the affinity constants for the labeled T2G1s were similar across different fragments, suggesting only one of the binding domains interacts with fibrin, despite fibrin having two sites for binding.
Article Abstract
Immunoreactivity of radiolabeled F(ab')2 fragment of anti-fibrin T2G1s monoclonal antibody was determined by affinity chromatography using fibrin-coated Sepharose. This preparation is useful for thrombus detection in vivo by gamma camera imaging, provided a high percentage of immunoreactivity is retained after labeling. For 111In labeling, DTPA/F(ab')2 molar ratios were varied from 1000 to 6600/1, with little effect on immunoreactivity. Immunoreactivity of the F(ab')2 fragment, labeled with imaging doses of 131I and 111In, remained high and ranged from 81% to 89%. Equilibrium binding analysis determined the affinity constants of 111In- or 125I-labeled T2G1s and its F(ab')2 and Fab fragments, to be equivalent (Kd approximately 3 X 10(-8) M). This suggests that only one binding domain of T2G1s binds to fibrin even though there are two antigenic sites/mol of fibrin.
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| http://dx.doi.org/10.1016/0022-1759(89)90320-7 | DOI Listing |
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