Detection of acyl esterase activity on electrophoresis membranes and separation from hyaluronidase
A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acety...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1975 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Analytical Biochemistry - Amsterdam : Elsevier, 68(1975), 1, Seite 218-225 |
| Übergeordnetes Werk: |
volume:68 ; year:1975 ; number:1 ; pages:218-225 |
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| 520 | |a A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. | ||
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(DE-627)NLEJ177252448 (DE-599)GBVNLZ177252448 DE-627 ger DE-627 rakwb eng Detection of acyl esterase activity on electrophoresis membranes and separation from hyaluronidase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herd, J.K. oth Tschida, J. oth in Analytical Biochemistry Amsterdam : Elsevier 68(1975), 1, Seite 218-225 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:68 year:1975 number:1 pages:218-225 http://dx.doi.org/10.1016/0003-2697(75)90697-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1975 1 218-225 |
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(DE-627)NLEJ177252448 (DE-599)GBVNLZ177252448 DE-627 ger DE-627 rakwb eng Detection of acyl esterase activity on electrophoresis membranes and separation from hyaluronidase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herd, J.K. oth Tschida, J. oth in Analytical Biochemistry Amsterdam : Elsevier 68(1975), 1, Seite 218-225 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:68 year:1975 number:1 pages:218-225 http://dx.doi.org/10.1016/0003-2697(75)90697-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1975 1 218-225 |
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(DE-627)NLEJ177252448 (DE-599)GBVNLZ177252448 DE-627 ger DE-627 rakwb eng Detection of acyl esterase activity on electrophoresis membranes and separation from hyaluronidase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herd, J.K. oth Tschida, J. oth in Analytical Biochemistry Amsterdam : Elsevier 68(1975), 1, Seite 218-225 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:68 year:1975 number:1 pages:218-225 http://dx.doi.org/10.1016/0003-2697(75)90697-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1975 1 218-225 |
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(DE-627)NLEJ177252448 (DE-599)GBVNLZ177252448 DE-627 ger DE-627 rakwb eng Detection of acyl esterase activity on electrophoresis membranes and separation from hyaluronidase 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herd, J.K. oth Tschida, J. oth in Analytical Biochemistry Amsterdam : Elsevier 68(1975), 1, Seite 218-225 (DE-627)NLEJ17685830X (DE-600)1461105-3 0003-2697 nnns volume:68 year:1975 number:1 pages:218-225 http://dx.doi.org/10.1016/0003-2697(75)90697-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1975 1 218-225 |
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detection of acyl esterase activity on electrophoresis membranes and separation from hyaluronidase |
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Detection of acyl esterase activity on electrophoresis membranes and separation from hyaluronidase |
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A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. |
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A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. |
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A method is described for the detection of acyl esterase activity on cellulose acetate membranes following electrophoresis of the enzyme. It uses the indigogenic substrate, indoxyl acetate, which directly forms the colored product visualized in the test. This substrate also detects activity of acetyl cholinesterase and pseudocholinesterase. With this method, bovine testicular hyaluronidase is shown to contain acyl esterase activity. By electrophoresis of hyaluronidase preparations at pH 6.8, esterase and hyaluronidase activities are separated, further assuring the specificity of the method for hyaluronidase. |
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