Journal article
Site‐directed mutagenesis of the P2 residue of human antithrombin
Abstract
Antithrombin (AT) is the principal inhibitor of thrombin in human plasma, and a member of the serine proteinase (serpin) family of proteins. Previously, we have described a point mutation in the human AT gene that converted amino acid 392 from glycine to aspartic acid which was associated with thrombotic disease in a Swedish family [(1992) Blood 79, 1428-1434]. This observation prompted us to investigate the consequences of other substitutions …
Authors
Sheffield WP; Blajchman MA
Journal
FEBS Letters, Vol. 339, No. 1-2, pp. 147–150
Publisher
Wiley
Publication Date
February 14, 1994
DOI
10.1016/0014-5793(94)80403-6
ISSN
0014-5793