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A new familial variant of antithrombin III: ‘Antithrombin III Paris’
Author(s) -
Wolf M.,
Boyer C.,
Lavergne J. M.,
Larrieu M. J.
Publication year - 1982
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1982.tb02782.x
Subject(s) - antithrombin , heparin , immunoelectrophoresis , asymptomatic , chemistry , affinity chromatography , agarose , antigen , medicine , biochemistry , immunology , endocrinology , enzyme
S ummary . A 59‐year‐old woman presented a recurrent history of thromboembolism. A qualitative defect of antithrombin III (AT III) was suggested by the discrepancy between a normal amount of AT III antigen and a decreased heparin cofactor activity. Six members of the same family showed a similar defect although clinically asymptomatic. The qualitative abnormality of AT III was confirmed by two‐dimensional immunoelectrophoresis. In the absence of heparin, a single peak was obtained with both control and patients' plasmas. In the presence of heparin, two peaks of AT III were observed in the patients' plasmas: the mobility of one peak was similar to that of the control, whereas the other showed a decreased mobility, suggesting a lack of binding to heparin. The two populations of AT III were separated by affinity chromatography on heparin‐agarose. 50% of the patients' AT III bound to the agarose beads. The remainder, recovered in the supernatant, migrated in two‐dimensional immunoelectrophoresis as a single peak with the same mobility in the presence or absence of heparin, and was devoid of heparin cofactor activity. This familial AT III variant characterized by a reduced affinity for heparin is tentatively named ‘Antithrombin III Paris’.