Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms
Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molec...
Ausführliche Beschreibung
Gespeichert in:
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1983 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 226(1983), 2, Seite 414-424 |
| Übergeordnetes Werk: |
volume:226 ; year:1983 ; number:2 ; pages:414-424 |
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| 245 | 1 | 0 | |a Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms |
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| 520 | |a Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. | ||
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(DE-627)NLEJ183811941 (DE-599)GBVNLZ183811941 DE-627 ger DE-627 rakwb eng Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Manao, G. oth Camici, G. oth Stefani, M. oth Berti, A. oth Cappugi, G. oth Liguri, G. oth Nassi, P. oth Ramponi, G. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 226(1983), 2, Seite 414-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:226 year:1983 number:2 pages:414-424 http://dx.doi.org/10.1016/0003-9861(83)90310-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 226 1983 2 414-424 |
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(DE-627)NLEJ183811941 (DE-599)GBVNLZ183811941 DE-627 ger DE-627 rakwb eng Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Manao, G. oth Camici, G. oth Stefani, M. oth Berti, A. oth Cappugi, G. oth Liguri, G. oth Nassi, P. oth Ramponi, G. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 226(1983), 2, Seite 414-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:226 year:1983 number:2 pages:414-424 http://dx.doi.org/10.1016/0003-9861(83)90310-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 226 1983 2 414-424 |
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(DE-627)NLEJ183811941 (DE-599)GBVNLZ183811941 DE-627 ger DE-627 rakwb eng Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Manao, G. oth Camici, G. oth Stefani, M. oth Berti, A. oth Cappugi, G. oth Liguri, G. oth Nassi, P. oth Ramponi, G. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 226(1983), 2, Seite 414-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:226 year:1983 number:2 pages:414-424 http://dx.doi.org/10.1016/0003-9861(83)90310-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 226 1983 2 414-424 |
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(DE-627)NLEJ183811941 (DE-599)GBVNLZ183811941 DE-627 ger DE-627 rakwb eng Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Manao, G. oth Camici, G. oth Stefani, M. oth Berti, A. oth Cappugi, G. oth Liguri, G. oth Nassi, P. oth Ramponi, G. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 226(1983), 2, Seite 414-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:226 year:1983 number:2 pages:414-424 http://dx.doi.org/10.1016/0003-9861(83)90310-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 226 1983 2 414-424 |
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(DE-627)NLEJ183811941 (DE-599)GBVNLZ183811941 DE-627 ger DE-627 rakwb eng Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Manao, G. oth Camici, G. oth Stefani, M. oth Berti, A. oth Cappugi, G. oth Liguri, G. oth Nassi, P. oth Ramponi, G. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 226(1983), 2, Seite 414-424 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:226 year:1983 number:2 pages:414-424 http://dx.doi.org/10.1016/0003-9861(83)90310-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 226 1983 2 414-424 |
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affinity chromatographic purification of horse muscle acylphosphatase: evidence of the existence of multiple molecular forms |
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Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms |
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Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. |
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Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. |
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Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate. |
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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">NLEJ183811941</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706213220.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1983 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183811941</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183811941</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">Affinity chromatographic purification of horse muscle acylphosphatase: Evidence of the existence of multiple molecular forms</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1983</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">Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) SS bound to the sole cysteine present at position 21 of the main chain. Ho3 is an SS dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate.</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">Manao, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Camici, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Stefani, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berti, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cappugi, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Liguri, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Nassi, P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ramponi, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Archives of Biochemistry and Biophysics</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">226(1983), 2, Seite 414-424</subfield><subfield code="w">(DE-627)NLEJ177020539</subfield><subfield code="w">(DE-600)1461378-5</subfield><subfield code="x">0003-9861</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:226</subfield><subfield code="g">year:1983</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:414-424</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-9861(83)90310-7</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">226</subfield><subfield code="j">1983</subfield><subfield code="e">2</subfield><subfield code="h">414-424</subfield></datafield></record></collection>
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