A new ultrasensitive method for the determination of proteolytic activity
An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagena...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1968 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Clinica Chimica Acta - Amsterdam : Elsevier, 21(1968), 2, Seite 197-203 |
| Übergeordnetes Werk: |
volume:21 ; year:1968 ; number:2 ; pages:197-203 |
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NLEJ186145845 |
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| 245 | 1 | 2 | |a A new ultrasensitive method for the determination of proteolytic activity |
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| 520 | |a An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. | ||
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| 700 | 1 | |a Rinderknecht, H. |4 oth | |
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| 700 | 1 | |a Silverman, P. |4 oth | |
| 700 | 1 | |a Haverback, B.J. |4 oth | |
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(DE-627)NLEJ186145845 (DE-599)GBVNLZ186145845 DE-627 ger DE-627 rakwb eng A new ultrasensitive method for the determination of proteolytic activity 1968 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Geokas, M.C. oth Silverman, P. oth Haverback, B.J. oth in Clinica Chimica Acta Amsterdam : Elsevier 21(1968), 2, Seite 197-203 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:21 year:1968 number:2 pages:197-203 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(68)90127-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1968 2 197-203 |
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(DE-627)NLEJ186145845 (DE-599)GBVNLZ186145845 DE-627 ger DE-627 rakwb eng A new ultrasensitive method for the determination of proteolytic activity 1968 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Geokas, M.C. oth Silverman, P. oth Haverback, B.J. oth in Clinica Chimica Acta Amsterdam : Elsevier 21(1968), 2, Seite 197-203 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:21 year:1968 number:2 pages:197-203 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(68)90127-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1968 2 197-203 |
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(DE-627)NLEJ186145845 (DE-599)GBVNLZ186145845 DE-627 ger DE-627 rakwb eng A new ultrasensitive method for the determination of proteolytic activity 1968 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Geokas, M.C. oth Silverman, P. oth Haverback, B.J. oth in Clinica Chimica Acta Amsterdam : Elsevier 21(1968), 2, Seite 197-203 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:21 year:1968 number:2 pages:197-203 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(68)90127-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1968 2 197-203 |
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(DE-627)NLEJ186145845 (DE-599)GBVNLZ186145845 DE-627 ger DE-627 rakwb eng A new ultrasensitive method for the determination of proteolytic activity 1968 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Geokas, M.C. oth Silverman, P. oth Haverback, B.J. oth in Clinica Chimica Acta Amsterdam : Elsevier 21(1968), 2, Seite 197-203 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:21 year:1968 number:2 pages:197-203 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(68)90127-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1968 2 197-203 |
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(DE-627)NLEJ186145845 (DE-599)GBVNLZ186145845 DE-627 ger DE-627 rakwb eng A new ultrasensitive method for the determination of proteolytic activity 1968 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rinderknecht, H. oth Geokas, M.C. oth Silverman, P. oth Haverback, B.J. oth in Clinica Chimica Acta Amsterdam : Elsevier 21(1968), 2, Seite 197-203 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:21 year:1968 number:2 pages:197-203 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(68)90127-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 21 1968 2 197-203 |
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An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. |
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An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. |
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An ultrasensitive method for the colorimetric determination of proteolytic activity in biological fluids is described. It is based on an insoluble substrate derived from hide powder labeled covalently with Remazolbrilliant Blue. All of six proteases tested: trypsin, chymotrypsin, elastase, collagenase, fibrinolysin and pepsin can be determined at concentrations of 50-100 ng/ml incubation mixture. Trypsin, fibrinolysin and elastase can still be estimated at concentrations as low as 1-2 ng/ml assay mixture. In contrast to other insoluble, non-covalent protein-dye complexes in use for the determination of proteolytic activity, the new chromogenic substrates are not affected by the presence of albumin. |
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