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An inhibitor of plasminogen activator was purified to apparent homogeneity from human umbilical vein endothelial cell conditioned medium. The purification was achieved by a speedy and simple two-step procedure, without the use of denaturants. The purified protein was a single-chain glycoprotein with apparent molecular mass of 48 kDa. The purified inhibitor had a specific activity of 8500 U/mg protein and the activity could be stimulated about fourteenfold by treatment with denaturants. An antiserum to the purified inhibitor was raised in rabbits. It recognised plasminogen activator inhibitor from platelets and plasma as well as from cultured endothelial cells. The immunoglobulin fraction of the antiserum neutralised the functional activity of the inhibitor from all these sources.
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
December 1988,
Biochemistry and cell biology = Biochimie et biologie cellulaire,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
September 1979,
Biochimica et biophysica acta,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
July 1989,
Chemical & pharmaceutical bulletin,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
December 1986,
The Journal of clinical investigation,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
November 1984,
Biochimica et biophysica acta,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
April 1981,
Thrombosis and haemostasis,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
November 1987,
Biochemistry,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
March 1986,
Thrombosis research,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
April 1994,
Thrombosis research,
N A Booth, and
I R MacGregor, and
N R Hunter, and
B Bennett
December 1984,
The Journal of biological chemistry,
