Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity
1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by dival...
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Englisch |
| Erschienen: |
1971 |
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Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: BBA - Enzymology - Amsterdam : Elsevier, 235(1971), 2, Seite 343-352 |
| Übergeordnetes Werk: |
volume:235 ; year:1971 ; number:2 ; pages:343-352 |
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| 520 | |a 1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). | ||
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(DE-627)NLEJ185792855 (DE-599)GBVNLZ185792855 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zelinkova, E. oth Bacova, M. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 343-352 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:343-352 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90213-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 343-352 |
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(DE-627)NLEJ185792855 (DE-599)GBVNLZ185792855 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zelinkova, E. oth Bacova, M. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 343-352 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:343-352 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90213-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 343-352 |
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(DE-627)NLEJ185792855 (DE-599)GBVNLZ185792855 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zelinkova, E. oth Bacova, M. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 343-352 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:343-352 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90213-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 343-352 |
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(DE-627)NLEJ185792855 (DE-599)GBVNLZ185792855 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zelinkova, E. oth Bacova, M. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 343-352 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:343-352 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90213-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 343-352 |
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(DE-627)NLEJ185792855 (DE-599)GBVNLZ185792855 DE-627 ger DE-627 rakwb eng Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zelinkova, E. oth Bacova, M. oth Zelinka, J. oth in BBA - Enzymology Amsterdam : Elsevier 235(1971), 2, Seite 343-352 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:235 year:1971 number:2 pages:343-352 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90213-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 235 1971 2 343-352 |
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exocellular ribonuclease from streptomyces aureofaciens ii. properties and specificity |
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Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity |
| abstract |
1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). |
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1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). |
| abstract_unstemmed |
1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26). |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ185792855</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707025419.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1971 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185792855</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185792855</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Exocellular ribonuclease from Streptomyces aureofaciens II. Properties and specificity</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1971</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">1. Properties and specificity of exocellular ribonuclease from Streptomyces aureofaciens BM-K, a strain producing the antibiotic chlortetracycline, were studied. The enzyme had maximal activity at pH 7.0. The optimal temperature has been found to be around 45^o.2. Ribonuclease was inhibited by divalent cations Cu^2^+ and Zn^2^+ and by increasing ionic strength.3. The enzyme was relatively heat-stable, the highest stability was observed at pH 7.0. At acidic pH values, the enzyme retained relatively high activity; at basic pH values (about 12) the loss of the activity was nearly 100%.4. The ribonuclease hydrolyzed yeast RNA to the only mononucleotide, guanosine 3'-phosphate, forming guanosine 2',3'-cyclic phosphate as intermediate, and to the oligonucleotides with terminal guanosine 3'-phosphate.5. Polyguanylic and polyinosinic acids, but not polyadenylic, polyuridylic and polycytidylic acids, were split by the low ribonuclease activity.6. In excess the ribonuclease hydrolyzed polyadenylic acid, as well as polyguanylic and polyinosinic acids, partially hydrolyzed polyuridylic acids.7. From these results it was concluded that Streptomyces aureofaciens ribonuclease was an endonuclease specific for guanosine 3'-phosphate, similar to the ribonuclease T"1 (ribonucleate 2'-guaninenucleotido-2'-transferase (cyclising, EC 2.7.7.26).</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zelinkova, E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bacova, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zelinka, J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">BBA - Enzymology</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">235(1971), 2, Seite 343-352</subfield><subfield code="w">(DE-627)NLEJ185751202</subfield><subfield code="w">(DE-600)2209533-0</subfield><subfield code="x">0005-2744</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:235</subfield><subfield code="g">year:1971</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:343-352</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2744(71)90213-0</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">235</subfield><subfield code="j">1971</subfield><subfield code="e">2</subfield><subfield code="h">343-352</subfield></datafield></record></collection>
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