A new spectrophotometric arginase assay
We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1967 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Analytical Biochemistry - Amsterdam : Elsevier, 18(1967), 1, Seite 102-106 |
| Übergeordnetes Werk: |
volume:18 ; year:1967 ; number:1 ; pages:102-106 |
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| 520 | |a We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. | ||
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(DE-627)NLEJ183926250 (DE-599)GBVNLZ183926250 DE-627 ger DE-627 rakwb eng A new spectrophotometric arginase assay 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Srere, P.A. oth in Analytical Biochemistry Amsterdam : Elsevier 18(1967), 1, Seite 102-106 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:18 year:1967 number:1 pages:102-106 http://dx.doi.org/10.1016/0003-2697(67)90062-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 18 1967 1 102-106 |
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(DE-627)NLEJ183926250 (DE-599)GBVNLZ183926250 DE-627 ger DE-627 rakwb eng A new spectrophotometric arginase assay 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Srere, P.A. oth in Analytical Biochemistry Amsterdam : Elsevier 18(1967), 1, Seite 102-106 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:18 year:1967 number:1 pages:102-106 http://dx.doi.org/10.1016/0003-2697(67)90062-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 18 1967 1 102-106 |
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(DE-627)NLEJ183926250 (DE-599)GBVNLZ183926250 DE-627 ger DE-627 rakwb eng A new spectrophotometric arginase assay 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Srere, P.A. oth in Analytical Biochemistry Amsterdam : Elsevier 18(1967), 1, Seite 102-106 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:18 year:1967 number:1 pages:102-106 http://dx.doi.org/10.1016/0003-2697(67)90062-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 18 1967 1 102-106 |
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(DE-627)NLEJ183926250 (DE-599)GBVNLZ183926250 DE-627 ger DE-627 rakwb eng A new spectrophotometric arginase assay 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Srere, P.A. oth in Analytical Biochemistry Amsterdam : Elsevier 18(1967), 1, Seite 102-106 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:18 year:1967 number:1 pages:102-106 http://dx.doi.org/10.1016/0003-2697(67)90062-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 18 1967 1 102-106 |
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(DE-627)NLEJ183926250 (DE-599)GBVNLZ183926250 DE-627 ger DE-627 rakwb eng A new spectrophotometric arginase assay 1967 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ward, R.L. oth Srere, P.A. oth in Analytical Biochemistry Amsterdam : Elsevier 18(1967), 1, Seite 102-106 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:18 year:1967 number:1 pages:102-106 http://dx.doi.org/10.1016/0003-2697(67)90062-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 18 1967 1 102-106 |
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We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. |
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We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. |
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We wish to report a new method for the assay of arginase (l-arginine amidinohydrolase, EC 3.5.3.1).Arginase, the terminal enzyme of the urea-ornithine cycle (1), catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a colorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay is a spectrophotometric method based on the fact that the absorbancy of arginase below 2100 A is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity. |
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