Biomedical Engineering Reference
In-Depth Information
65. Wardell, M.R. et al., Crystallization and preliminary X-ray diffraction analysis of two conformations of
intact human antithrombin,
J. Mol. Biol
., 234, 1253, 1993.
66. Fleischer, B., Mechanism of glycosylation in the golgi apparatus,
J. Histochem. Cytochem
., 31, 1033,
1983.
67. Garone, L. et al., Antithrombin-heparin affi nity reduced by fucosylation of carbohydrate at asparagine
155,
Biochemistry
, 35, 8881, 1996.
68. Bjork, I. et al., Decreased affi nity of recombinant antithrombin for heparin due to increased glycosyl-
ation,
Biochem. J
., 286, 793, 1992.
69. Borsodi, A. and Narasimhan, T.R., Microheterogeneity of human antithrombin III,
Br. J. Haematol
.,
39, 121, 1978.
70. Witmer, M.R. and Hatton, M.W., Antithrombin III-beta associates more readily than antithrombin
III-alpha with uninjured and de-endothelialized aortic wall
in vitro
and
in vivo,
Arterioscler. Thromb
.,
11, 530, 1991.
71. Carlson, T.H., Kolman, M.R., and Piepkorn, M., Activation of antithrombin III isoforms by heparan sul-
phate glycosaminoglycans and other sulphated polysaccharides,
Blood Coagul. Fibrinol
., 6, 474, 1995.
72. Brennan, S.O. et al., New carbohydrate site in mutant antithrombin (7 Ile-Asn) with decreased heparin
affi nity,
FEBS Lett
., 237, 118, 1988.
73. Stibler, H., Holzbach, U., and Kristiansson, B., Isoforms and levels of transferrin, antithrombin, alpha(1)-
antitrypsin and thyroxine-binding globulin in 48 patients with carbohydrate-defi cient glycoprotein syn-
drome type I,
Scand. J. Clin. Lab. Invest
., 58, 55, 1998.
74. Picard, V., Ersdal-Badju, E., and Bock, S.C., Partial glycosylation of antithrombin III asparagine-135 is
caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible
for production of the beta-antithrombin III isoform with enhanced heparin affi nity,
Biochemistry
, 34,
8433, 1995.
75. Karlsson, G. and Winge, S., Separation between the alpha and beta forms of human antithrombin by
hydroxyapatite high-performance liquid chromatography,
Protein Expr. Purif
., 28, 196, 2003.
76. Turk, B. et al., The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-
antithrombin, decreases the heparin affi nity of the inhibitor by affecting the heparin-induced confor-
mational change,
Biochemistry
, 36, 6682, 1997.
77. Howell, W.H., The coagulation of blood, in
The Harvey Lectures
, Lippincott, Philadelphia, 1918, chap. 7.
78. Marcum, J.A., Howell, W.H., and McLean, J., The experimental context for the discovery of heparin,
Perspect. Biol. Med
., 33, 214, 1990.
79. Brinkhous, K. et al., The inhibition of blood clotting: An unidentifi ed substance which acts in conjunction
with heparin to prevent the conversion of prothrombin to thrombin,
Am. J. Physiol
., 125, 683, 1939.
80. Seegers, W.H., Johnson, J.F., and Fall, C., An antithrombin reaction related to prothrombin activation,
Am. J. Physiol
., 176, 97, 1954.
81. Devraj-Kizuk, R. et al., Antithrombin III-Hamilton: A gene with a point mutation (guanine to adenine)
in codon 382 causing impaired serine protease reactivity,
Blood
, 72, 1518, 1988.
82. Whinna, H.C. and Church, F.C., Interaction of thrombin with antithrombin, heparin cofactor II, and
protein C inhibitor,
J. Protein. Chem
., 12, 677, 1993.
83. Carrell, R.W. and Owen, M.C., Plakalbumin, a2-antitrypsin, antithrombin and the mechanism of infl am-
matory thrombosis,
Nature
, 317, 730, 1985.
84. Schulze, A.J. et al., Structural aspects of serpin inhibition,
FEBS Lett
., 344, 117, 1994.
85. Skriver, K. et al., Substrate properties of C1 inhibitor Ma (alanine 434—glutamic acid). Genetic and
structural evidence suggesting that the P12-region contains critical determinants of serine protease
inhibitor/substrate status,
J. Biol. Chem
., 266, 9216, 1991.
86. Schulze, A.J. et al., Structural transition of alpha-1-antitrypsin by a peptide sequentially similar to beta-
strand s4A,
Eur. J. Biochem
., 194, 51, 1990.
87. Schulze, A.J. et al., Evidence for the extent of insertion of the active site loop of intact alpha 1 proteinase
inhibitor in beta-sheet A,
Biochemistry
, 31, 7560, 1992.
88. Bjork, I. et al., Kinetic characterization of the substrate reaction between a complex of antithrombin
with a synthetic reactive-bond loop tetradecapeptide and four target proteinases of the inhibitor,
J. Biol.
Chem
., 267, 19 0 47, 1992.
89. Bjork, I. et al., Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced
heparin affi nity and enhanced conformational stability by binding of a tetradecapeptide corresponding
to the P1 to P14 region of the putative reactive bond loop of the inhibitor,
J. Biol. Chem
., 267,
1976, 1992.
