Effect of α"2 macroglobulin on some kinetic parameters of trypsin
1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed w...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1975 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA - Enzymology - Amsterdam : Elsevier, 377(1975), 1, Seite 158-165 |
| Übergeordnetes Werk: |
volume:377 ; year:1975 ; number:1 ; pages:158-165 |
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NLEJ185780768 |
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| 245 | 1 | 0 | |a Effect of α"2 macroglobulin on some kinetic parameters of trypsin |
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| 520 | |a 1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. | ||
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(DE-627)NLEJ185780768 (DE-599)GBVNLZ185780768 DE-627 ger DE-627 rakwb eng Effect of α"2 macroglobulin on some kinetic parameters of trypsin 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Fleming, R.M. oth Geokas, M.C. oth in BBA - Enzymology Amsterdam : Elsevier 377(1975), 1, Seite 158-165 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:377 year:1975 number:1 pages:158-165 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(75)90296-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 377 1975 1 158-165 |
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(DE-627)NLEJ185780768 (DE-599)GBVNLZ185780768 DE-627 ger DE-627 rakwb eng Effect of α"2 macroglobulin on some kinetic parameters of trypsin 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Fleming, R.M. oth Geokas, M.C. oth in BBA - Enzymology Amsterdam : Elsevier 377(1975), 1, Seite 158-165 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:377 year:1975 number:1 pages:158-165 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(75)90296-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 377 1975 1 158-165 |
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(DE-627)NLEJ185780768 (DE-599)GBVNLZ185780768 DE-627 ger DE-627 rakwb eng Effect of α"2 macroglobulin on some kinetic parameters of trypsin 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Fleming, R.M. oth Geokas, M.C. oth in BBA - Enzymology Amsterdam : Elsevier 377(1975), 1, Seite 158-165 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:377 year:1975 number:1 pages:158-165 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(75)90296-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 377 1975 1 158-165 |
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(DE-627)NLEJ185780768 (DE-599)GBVNLZ185780768 DE-627 ger DE-627 rakwb eng Effect of α"2 macroglobulin on some kinetic parameters of trypsin 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Fleming, R.M. oth Geokas, M.C. oth in BBA - Enzymology Amsterdam : Elsevier 377(1975), 1, Seite 158-165 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:377 year:1975 number:1 pages:158-165 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(75)90296-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 377 1975 1 158-165 |
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(DE-627)NLEJ185780768 (DE-599)GBVNLZ185780768 DE-627 ger DE-627 rakwb eng Effect of α"2 macroglobulin on some kinetic parameters of trypsin 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Fleming, R.M. oth Geokas, M.C. oth in BBA - Enzymology Amsterdam : Elsevier 377(1975), 1, Seite 158-165 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:377 year:1975 number:1 pages:158-165 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(75)90296-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 377 1975 1 158-165 |
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Effect of α"2 macroglobulin on some kinetic parameters of trypsin |
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1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. |
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1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. |
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1.|Complex formation of trypsin with α"2 macroglobulin results in marked changes of the Michaelis-Menten constant, pH optimum and sensitivity to ionic strength in a system using N-carbobenzoxy-glycylglycyl-l-arginine-2-naphthylamide as substrate.2.|In contrast to the inhibition (50%) observed when α"2 macroglobulin bound trypsin is assayed under conditions optimal for the free enzyme, there is minimal reduction of activity when determinations are performed at a substrate concentration and pH optimal for the bound enzyme.3.|The changes in substrate concentration and ionic environment required for maximum activity of α"2 macroglobulin-bound trypsin are similar to those observed with enzymes embedded in polyelectrolyte matrices and may reflect alterations in the microenvironment of the enzyme resulting from conformational changes of the macromolecule during interaction with trypsin.4.|Enzymatic activity of trypsin towards casein is greatly reduced by α"2 macroglobulin, even under assay conditions optimal for the bound enzyme, confirming previous findings that access to the active center for high-molecular weight substrates is sterically hindered by α"2 macroglobulin. |
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