Abstract:
:The molecular basis and functional properties of a variant antithrombin (AT) protein. AT Budapest 3, were studied. A single base substitution was identified in codon 99, CTC----TTC, altering the normal leucine to phenylalanine. The proband presented with a history of venous thrombotic disease and was found to be homozygous for the mutation. The variant protein demonstrated reduced heparin affinity and reduced antiproteinase activity in the presence of either unfractionated heparin or the AT-binding heparin pentasaccharide, when compared to normal AT. A small change in the isoelectric point was also identified. The substituted amino acid residue of AT Budapest 3 is located near to the proposed AT heparin binding site, and it is suggested that reduced heparin affinity of the variant protein may result from substitution-induced distortion of positive charge geometry in the binding site and/or changes in its position relative to the rest of the inhibitor molecule.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Olds RJ,Lane DA,Boisclair M,Sas G,Bock SC,Thein SLdoi
10.1016/0014-5793(92)80854-akeywords:
subject
Has Abstractpub_date
1992-04-06 00:00:00pages
241-6issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(92)80854-Ajournal_volume
300pub_type
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