Title : Isolation of multiple types of plasminogen activator inhibitors from vascular smooth muscle cells.

Pub. Date : 1989 Jun 30

PMID : 2799763






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Fractionation of VSMC-conditioned medium by heparin-affigel chromatography separated three immunologically and functionally distinct PA inhibitors (PAI), namely PAI-1, PAI-2 and protease-nexin I. Heparin serpin family E member 1 Homo sapiens
2 PA inhibitor 2 (PAI-2) had little affinity for heparin, whereas PA inhibitor 1 (PAI-1) bound to heparin and was eluted from the column at NaCl concentrations of 0.1 to 0.35 M. Protease-nexin I, eluted at NaCl concentrations of 0.5 M and higher. Heparin serpin family E member 1 Homo sapiens
3 PA inhibitor 2 (PAI-2) had little affinity for heparin, whereas PA inhibitor 1 (PAI-1) bound to heparin and was eluted from the column at NaCl concentrations of 0.1 to 0.35 M. Protease-nexin I, eluted at NaCl concentrations of 0.5 M and higher. Heparin serpin family E member 1 Homo sapiens
4 Thus, human VSMC produce all three presently known PAI and these can be separated in single heparin affinity purification step. Heparin serpin family E member 1 Homo sapiens