Exocellular ribonuclease from Streptomyces aureofaciens I. Isolation and purification
1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fraction...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1971 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA - Enzymology - Amsterdam : Elsevier, 235(1971), 2, Seite 335-342 |
| Übergeordnetes Werk: |
volume:235 ; year:1971 ; number:2 ; pages:335-342 |
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| 520 | |a 1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. | ||
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(DE-627)NLEJ185792847 (DE-599)GBVNLZ185792847 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens I. Isolation and purification 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bacova, M. oth Zelinkova, E. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 335-342 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:335-342 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90212-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 335-342 |
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(DE-627)NLEJ185792847 (DE-599)GBVNLZ185792847 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens I. Isolation and purification 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bacova, M. oth Zelinkova, E. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 335-342 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:335-342 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90212-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 335-342 |
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(DE-627)NLEJ185792847 (DE-599)GBVNLZ185792847 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens I. Isolation and purification 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bacova, M. oth Zelinkova, E. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 335-342 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:335-342 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90212-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 335-342 |
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(DE-627)NLEJ185792847 (DE-599)GBVNLZ185792847 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens I. Isolation and purification 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bacova, M. oth Zelinkova, E. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 335-342 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:335-342 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90212-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 335-342 |
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(DE-627)NLEJ185792847 (DE-599)GBVNLZ185792847 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens I. Isolation and purification 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bacova, M. oth Zelinkova, E. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 335-342 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:335-342 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90212-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 335-342 |
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exocellular ribonuclease from streptomyces aureofaciens i. isolation and purification |
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Exocellular ribonuclease from Streptomyces aureofaciens I. Isolation and purification |
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1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. |
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1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. |
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1. The ribonuclease from the cultural medium of Streptomyces aureofaciens BM-K, a chlorotetracycline-producing strain, was purified to a chromatographically and disc-electrophoretically homogeneous state. The enzyme was purified 1000-fold with a yield of 13% with the aid of ammonium sulfate fractionation and by chromatography on DEAE-Sephadex A-25 and DEAE-cellulose.2. The purified enzyme was found to be free of deoxyribonuclease, non-specific phosphodiesterase and monophosphatase activity.3. The amino acid composition of Streptomyces aureofaciens ribonuclease was determined.4. The isoelectric point was found to be around pH 4.3. |
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