Abstract:
:Antithrombin Glasgow is a hereditary abnormal antithrombin that has lost thrombin inhibitory activity. It was isolated from the plasma of a 41-year-old male with a history of thrombotic events. Antithrombin Glasgow was purified from plasma using heparin-Sepharose chromatography at pH 7.4 eluting with increasing concentrations of NaCl. The normal protein eluted with 0.9 mol/l NaCl and Glasgow with 1.05 mol/l NaCl. Electrophoresis in agarose at pH 8.6 showed the variant to migrate more anodally than normal. The C-terminal small fragment resulting from catalytic cleavage with elastase between P3 and P4 of the reactive loop was isolated and sequenced. This showed the replacement of the arginine at residue 3 by a histidine. This is residue 393 in the intact molecule. The findings suggest that heparin, on binding, interacts indirectly with the reactive centre region of antithrombin.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Owen MC,Beresford CH,Carrell RWdoi
10.1016/0014-5793(88)80841-xsubject
Has Abstractpub_date
1988-04-25 00:00:00pages
317-20issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(88)80841-Xjournal_volume
231pub_type
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