Detergent tween 80 modifies the specific activity of PAI-1

Fibrinolysis and Proteolysis

Volumn 11, Issue 3, 1997, Pages 165-170

  Ehnebom, J ^a   Bjorquist P ^a   Andersson, J O ^a   Johansson, T ^a   Deinum, J ^a  

^a ASTRAZENECA R AND D   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

PLASMINOGEN ACTIVATOR; POLYSORBATE 80;

ARTICLE; BLOOD CLOT LYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; HUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

EID: 0030720987     PISSN: 13690191     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0268-9499(97)80061-6     Document Type: Article

References (19)

1. Collen D. On the regulation and control of fibrinolysis. Thromb Haemost 1980; 43: 77-89.
2. Kruithof EKO, Ransijn A, Bachmann F. Influence of detergents on the measurements of the fibrinolytic activity of plasminogen activators. Thromb Res 1982; 8: 251-260.
3. Gettins P, Patston PA, Schapira M. Structure and mechanism of action of serpins. Hematology Oncology Clinics of North America 1992; 6(6): 1393-1408.
4. Declerck P J, De Mol M, Vaughan D E, Collen D. Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a non-inhibitory substrate for tissue-type plasminogen activator. J Biol Chem 1992; 267(17): 11693-11696.
5. Sancho E, Declerck P J, Price N C, Kelly S M, Booth N A. Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms. Biochemistry 1995; 34(3): 1064-1069.
6. Urano T, Strandberg L, Johansson LB-Å, Ny T. A substrate-like form of plasminogen-activator-inhibitor type 1. Eur J Biochem 1992; 209: 985-992.
7. Wiman B, Lindahl T, Almquist Å. Evidence for a discrete binding protein of plasminogen activator inhibitor in plasma. Thromb Haemost 1988; 59: 392-395.
8. Hekman CM, Loskutoff D J. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J Biol Chem 1985; 260: 11581-11587.
9. Boström S L, Deinum J, Löfroth J-E, Wirth M, Kubista M. Conformational differences between latent and active plasminogen inhibitor, PAI-1 : A spectroscopic study. Thromb Res 1990; 59: 851-858.
10. Strömqvist M, Andersson J-O, Boström S, et al. Separation of active and inactive forms of recombinant human plasminogen activator inhibitor type 1 (PAI-1) expressed in Chinese hamster ovary cells: comparison with native human PAI-1. Protein Exp Pur 1994; 5: 309-316.
11. Kvassman J-O, Shore J D. Purification of human plasminogen activator inhibitor (PAI-1) from Escherichia coli and separation of its active and latent forms by hydrophobic interaction chromatography. Fibrinolysis 1995; 9: 215-221.
12. Munch M, Heegaard C W, Andreasen P. Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor. Biochim Biophys Acta 1993; 1202: 29-37.
13. Neugebauer J M. Detergents: an overview. Meth Enzymol 1990; 182: 239-253.
14. Hjelmeland L M. The design and synthesis of detergents for membrane biochemistry. Meth Enzymol 1986; 124: 135-164.
15. Björquist P, Brohlin M, Ehnebom J, Ericsson M, Kristiansen C, Pohl G, Deinum J. Plasminogen activator inhibitor type-1 interacts exclusively with the proteinase domain of tissue plasminogen activator. Biochim Biophys Acta 1994; 1209: 191-202.
16. Lottenberg R, Jackson C M. Solution composition dependent variation in extinction coefficients for p-Nitroaniline. Biochim Biophys Acta 1983; 742: 558-564.
17. Strömqvist M, Andersson K-E, Björquist P, Andersson J-O, Byström M, Hansson L, Johansson T, Deinum J. Characterisation of the complex of plasminogen activator inhibitor type 1 with tissue-type plasminogen activator by mass spectrometry and size-exclusion chromatography. Biochim Biophys Acta 1996; 1295: 103-109.
18. Hopkins P C R, Stone S R. The contribution of the conserved hinge region residues of alpha 1-antitrypsin to its reaction with elastase. Biochemistry 1995; 34: 15872-15879.
19. Wright H T, Scarsdale J N. Structural basis for serpin inhibitor activity. Proteins 1995; 22: 210-225.