Increase in the Resistance of Plasmin to the Inactivation by α2-Plasmin Inhibitor on Incubation
Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Shimokawa, Mari [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1994 |
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| Schlagwörter: |
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| Anmerkung: |
© The Japan Society for Analytical Chemistry 1994 |
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| Übergeordnetes Werk: |
Enthalten in: Analytical sciences - [Cham] : Springer International Publishing, 1985, 10(1994), 4 vom: Aug., Seite 533-536 |
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| Übergeordnetes Werk: |
volume:10 ; year:1994 ; number:4 ; month:08 ; pages:533-536 |
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| DOI / URN: |
10.2116/analsci.10.533 |
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10.2116/analsci.10.533 doi (DE-627)SPR047512695 (SPR)analsci.10.533-e DE-627 ger DE-627 rakwb eng Shimokawa, Mari verfasserin aut Increase in the Resistance of Plasmin to the Inactivation by α2-Plasmin Inhibitor on Incubation 1994 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Japan Society for Analytical Chemistry 1994 Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. Plasmin (dpeaa)DE-He213 -plasmin inhibitor (dpeaa)DE-He213 affinity (dpeaa)DE-He213 PI-binding site (dpeaa)DE-He213 Kinoshita, Toshio aut Enthalten in Analytical sciences [Cham] : Springer International Publishing, 1985 10(1994), 4 vom: Aug., Seite 533-536 (DE-627)300895925 (DE-600)1483376-1 1348-2246 nnns volume:10 year:1994 number:4 month:08 pages:533-536 https://dx.doi.org/10.2116/analsci.10.533 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_250 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 1994 4 08 533-536 |
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10.2116/analsci.10.533 doi (DE-627)SPR047512695 (SPR)analsci.10.533-e DE-627 ger DE-627 rakwb eng Shimokawa, Mari verfasserin aut Increase in the Resistance of Plasmin to the Inactivation by α2-Plasmin Inhibitor on Incubation 1994 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Japan Society for Analytical Chemistry 1994 Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. Plasmin (dpeaa)DE-He213 -plasmin inhibitor (dpeaa)DE-He213 affinity (dpeaa)DE-He213 PI-binding site (dpeaa)DE-He213 Kinoshita, Toshio aut Enthalten in Analytical sciences [Cham] : Springer International Publishing, 1985 10(1994), 4 vom: Aug., Seite 533-536 (DE-627)300895925 (DE-600)1483376-1 1348-2246 nnns volume:10 year:1994 number:4 month:08 pages:533-536 https://dx.doi.org/10.2116/analsci.10.533 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_250 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 1994 4 08 533-536 |
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10.2116/analsci.10.533 doi (DE-627)SPR047512695 (SPR)analsci.10.533-e DE-627 ger DE-627 rakwb eng Shimokawa, Mari verfasserin aut Increase in the Resistance of Plasmin to the Inactivation by α2-Plasmin Inhibitor on Incubation 1994 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Japan Society for Analytical Chemistry 1994 Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. Plasmin (dpeaa)DE-He213 -plasmin inhibitor (dpeaa)DE-He213 affinity (dpeaa)DE-He213 PI-binding site (dpeaa)DE-He213 Kinoshita, Toshio aut Enthalten in Analytical sciences [Cham] : Springer International Publishing, 1985 10(1994), 4 vom: Aug., Seite 533-536 (DE-627)300895925 (DE-600)1483376-1 1348-2246 nnns volume:10 year:1994 number:4 month:08 pages:533-536 https://dx.doi.org/10.2116/analsci.10.533 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_250 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 1994 4 08 533-536 |
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10.2116/analsci.10.533 doi (DE-627)SPR047512695 (SPR)analsci.10.533-e DE-627 ger DE-627 rakwb eng Shimokawa, Mari verfasserin aut Increase in the Resistance of Plasmin to the Inactivation by α2-Plasmin Inhibitor on Incubation 1994 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Japan Society for Analytical Chemistry 1994 Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. Plasmin (dpeaa)DE-He213 -plasmin inhibitor (dpeaa)DE-He213 affinity (dpeaa)DE-He213 PI-binding site (dpeaa)DE-He213 Kinoshita, Toshio aut Enthalten in Analytical sciences [Cham] : Springer International Publishing, 1985 10(1994), 4 vom: Aug., Seite 533-536 (DE-627)300895925 (DE-600)1483376-1 1348-2246 nnns volume:10 year:1994 number:4 month:08 pages:533-536 https://dx.doi.org/10.2116/analsci.10.533 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_250 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 1994 4 08 533-536 |
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10.2116/analsci.10.533 doi (DE-627)SPR047512695 (SPR)analsci.10.533-e DE-627 ger DE-627 rakwb eng Shimokawa, Mari verfasserin aut Increase in the Resistance of Plasmin to the Inactivation by α2-Plasmin Inhibitor on Incubation 1994 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Japan Society for Analytical Chemistry 1994 Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. Plasmin (dpeaa)DE-He213 -plasmin inhibitor (dpeaa)DE-He213 affinity (dpeaa)DE-He213 PI-binding site (dpeaa)DE-He213 Kinoshita, Toshio aut Enthalten in Analytical sciences [Cham] : Springer International Publishing, 1985 10(1994), 4 vom: Aug., Seite 533-536 (DE-627)300895925 (DE-600)1483376-1 1348-2246 nnns volume:10 year:1994 number:4 month:08 pages:533-536 https://dx.doi.org/10.2116/analsci.10.533 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_250 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 1994 4 08 533-536 |
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increase in the resistance of plasmin to the inactivation by α2-plasmin inhibitor on incubation |
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Increase in the Resistance of Plasmin to the Inactivation by α2-Plasmin Inhibitor on Incubation |
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Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. © The Japan Society for Analytical Chemistry 1994 |
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Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. © The Japan Society for Analytical Chemistry 1994 |
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Abstract Plasmin was found to acquire resistance to the inhibition by α2-plasmin inhibitor (α2PI) on incubation at 37°C in 50% glycerin whereas its amidase activity was preserved. This resistance is ascribable to the reduction of the affinity of plasmin to α2PI, since the ability of plasmin to form the complex with α2PI was proved to decrease on incubation. The reduced affinity of pre-incubated plasmin was recovered by incubation with α2PI. The pre-incubation presumably causes a reversible change in the conformation of the α2PI-binding site of plasmin. The use of freshly prepared plasmin solution is recommended for the assay of plasma α2PI if such an acquired resistance of plasmin is undesirable. © The Japan Society for Analytical Chemistry 1994 |
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