Biomedical Engineering Reference
In-Depth Information
39. Young, E. et al., Heparin binding to plasma proteins, an important mechanism for heparin resistance,
Thromb. Haemost ., 67, 639, 1992.
40. Jaques, L.B., Mahadoo, J., and Kavanagh, L.W., Intrapulmonary heparin: A new procedure for antico-
agulant therapy, Lancet , 7996, 1157, 1976.
41. Hirsh, J. et al., Heparin kinetics in venous thrombosis and pulmonary embolism, Circulation ,
53, 691, 1976.
42. Eisenberg, P. et al., Importance of factor Xa in determining the procoagulant activity of whole-blood
clots, J. Clin. Invest ., 91, 1877, 1993.
43. Prager, N.A. et al., Role of thrombin compared with factor Xa in the procoagulant activity of whole
blood clots, Circulation , 92, 962, 1995.
44. Weitz, J.I. et al., Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is
susceptible to inactivation by antithrombin III independent inhibitors, J. Clin. Invest ., 86, 385, 1990.
45. Hogg, P.J. and Jackson, C.M., Fibrin monomer protects thrombin from inactivation by heparin-
antithrombin III: Implications for heparin effi cacy, Proc. Natl Acad. Sci. USA , 86, 3619, 1989.
46. Theroux, P. et al., Reactivation of unstable angina after the discontinuation of heparin, N. Engl. J. Med .,
327, 192, 1992.
47. Palm, M. et al., Bleeding times in rats treated with heparin, heparin fragments of high and low anti-
coagulant activity and chemically modifi ed heparin fragments of low anticoagulant activity, Thromb.
Haemost ., 64, 127, 1990.
48. Kristensen, E.M. et al., Heparin coating durability on artifi cial heart valves studied by XPS and anti-
thrombin binding capacity, Colloids Surf. B. Biointerfaces , 49, 1, 2006.
49. Hatton, M.W.C. et al., Tritiation of commercial heparins by reaction with NaB3H4: Chemical analysis
and biological properties of the product, Anal. Biochem ., 106, 417, 1980.
50. Hunt, L.T. and Dayhoff, M.O., A surprising new protein superfamily containing ovalbumin, antithrom-
bin-III, and alpha 1-protease inhibitor, Biochem. Biophys. Res. Comm ., 95, 864, 1980.
51. Carrell, R.W. et al., Active site of a1-antitrypsin: Homologous site in antithrombin-III, Biochem.
Biophys. Res. Comm ., 93, 399, 1980.
52. Chandra, T. et al., Sequence homology between human alpha-1-antichymotrypsin, alpha-1-antitrypsin
and antithrombin III, Biochemistry , 22, 5055, 1983.
53. Carrell, R.W., Christey, P.B., and Boswell, D.R., Serpins: Antithrombin and other inhibitors of coagula-
tion and fi brinolysis: Evidence from amino acid sequences, in Thrombosis and Haemostasis , Verstraete,
M., Vermylen, J., and Lijnen, R., Eds., Leuven University Press, Leuven, Belgium, 1987, chap. 1.
54. Takano, T. et al., Interstitial deletion of chromosome 1q [del(1)(q24q25.3)] identifi ed by fl uorescence in
situ hybridization and gene dosage analysis of apolipoprotein A-II, coagulation factor V, and antithrom-
bin III, Am. J. Med. Genet ., 68, 207, 1997.
55. Bock, S.C., Marrinan, J.A., and Radziejewska, E., Antithrombin III Utah: Proline-407 to leucine muta-
tion in a highly conserved region near the inhibitor reactive site, Biochemistry , 27, 6171, 1988.
56. Prochownik, E.V., Bock, S.C., and Orkin, S.H., Intron structure of the human antithrombin III gene
differs from that of other members of the serine protease inhibitor superfamily, J. Biol. Chem ., 260,
9608, 1985.
57. Niessen, R.W. et al., Sequence characterization of a sheep cDNA for antithrombin III, Biochim.
Biophys. Acta , 1171, 207, 1992.
58. Abildgaard, U., Purifi cation of two progressive antithrombins of human plasma, Scand. J. Clin. Lab.
Invest ., 19, 190, 1967.
59. Rosenberg, R.D. and Damus, P.S., The purifi cation and mechanism of action of human antithrombin-
heparin cofactor, J. Biol. Chem ., 248, 6490, 1973.
60. Miller-Andersson, J., Borg, H., and Andersson, L.O., Purifi cation of antithrombin III by affi nity chro-
matography, Thromb. Res ., 5, 439, 1974.
61. Manson, H.E. et al., The molecular pathology of inherited human antithrombin III defi ciency, Tra nsf us.
Med. Rev ., 3, 264, 1989.
62. Villaneuva, G.B., Predictions of the secondary structure of antithrombin III and the location of the
heparin-binding site, J. Biol. Chem ., 259, 2531, 1984.
63. Petersen, T.E. et al., Primary structure of antithrombin III (heparin cofactor). Partial homology between
a1-antitrypsin and antithrombin III, in The Physiological Inhibitors of Coagulation and Fibrinolysis ,
Collen, D., Wiman, B., and Verstraete, M., Eds., Elsevier, Amsterdam, The Netherlands, 1979, chap. 2.
64. Carrell, R.W. et al., Biological implications of a 3A structure of dimeric antithrombin, Structure ,
2, 257, 1994.
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