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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by George, P. M. Articles by Barr, P. J. Search for Related Content PubMed PubMed Citation Articles by George, P. M. Articles by Barr, P. J. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast PM George, P Pemberton, IC Bathurst, RW Carrell, HL Gibson, S Rosenberg, RA Hallewell and PJ Barr Department of Pathology, Christchurch Hospital, New Zealand. Both congenital and acquired antithrombin-III (AT-III) deficiencies are amenable to replacement therapy. We describe two antithrombins produced by recombinant DNA techniques from human alpha 1-antitrypsin (alpha 1AT) cDNA in yeast. Alteration of the alpha 1AT active site, replacing methionine 358 with arginine, results in a thrombin inhibition rate similar to that of heparin-activated AT-III. Alteration of two further residues, to give a five-residue sequence identical to AT-III, does not increase this rate further. Neither antithrombin is activated by heparin; both are unglycosylated and have shorter in vivo half-lives (t1/2) than human alpha 1AT. These antithrombins should be suitable for therapeutic replacement of AT-III in cases of congenital deficiency and in conditions associated with acquired AT-III deficiency, such as disseminated intravascular coagulation. Volume 73, Issue 2, pp. 490-496, 02/01/1989 Copyright © 1989 by The American Society of Hematology CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: P. A. Pemberton, D. T. Wong, H. L. Gibson, M. C. Kiefer, P. A. Fitzpatrick, R. Sager, and P. J. Barr The Tumor Suppressor Maspin Does Not Undergo the Stressed to Relaxed Transition or Inhibit Trypsin-like Serine Proteases J. Biol. Chem., June 30, 1995; 270(26): 15832 - 15837. [Abstract] [Full Text] [PDF]

	Copyright © 1989 by American Society of Hematology         Online ISSN: 1528-0020