Expanded bed adsorption on supermacroporous cross-linked cellulose matrix
Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, p...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Pai, Anita [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1999 |
|---|
| Anmerkung: |
© Kluwer Academic Publishers 1999 |
|---|
| Übergeordnetes Werk: |
Enthalten in: Bioseparation - Kluwer Academic Publishers, 1990, 8(1999), 1-5 vom: Jan., Seite 131-138 |
|---|---|
| Übergeordnetes Werk: |
volume:8 ; year:1999 ; number:1-5 ; month:01 ; pages:131-138 |
| Links: |
|---|
| DOI / URN: |
10.1023/A:1008162829755 |
|---|
| Katalog-ID: |
OLC2050511760 |
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| 520 | |a Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. | ||
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10.1023/A:1008162829755 doi (DE-627)OLC2050511760 (DE-He213)A:1008162829755-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Pai, Anita verfasserin aut Expanded bed adsorption on supermacroporous cross-linked cellulose matrix 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. Gondkar, Shyamal aut Sundaram, Sumati aut Lali, Arvind aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 1-5 vom: Jan., Seite 131-138 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:1-5 month:01 pages:131-138 https://doi.org/10.1023/A:1008162829755 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 1-5 01 131-138 |
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10.1023/A:1008162829755 doi (DE-627)OLC2050511760 (DE-He213)A:1008162829755-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Pai, Anita verfasserin aut Expanded bed adsorption on supermacroporous cross-linked cellulose matrix 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. Gondkar, Shyamal aut Sundaram, Sumati aut Lali, Arvind aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 1-5 vom: Jan., Seite 131-138 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:1-5 month:01 pages:131-138 https://doi.org/10.1023/A:1008162829755 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 1-5 01 131-138 |
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10.1023/A:1008162829755 doi (DE-627)OLC2050511760 (DE-He213)A:1008162829755-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Pai, Anita verfasserin aut Expanded bed adsorption on supermacroporous cross-linked cellulose matrix 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. Gondkar, Shyamal aut Sundaram, Sumati aut Lali, Arvind aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 1-5 vom: Jan., Seite 131-138 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:1-5 month:01 pages:131-138 https://doi.org/10.1023/A:1008162829755 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 1-5 01 131-138 |
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10.1023/A:1008162829755 doi (DE-627)OLC2050511760 (DE-He213)A:1008162829755-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Pai, Anita verfasserin aut Expanded bed adsorption on supermacroporous cross-linked cellulose matrix 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. Gondkar, Shyamal aut Sundaram, Sumati aut Lali, Arvind aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 1-5 vom: Jan., Seite 131-138 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:1-5 month:01 pages:131-138 https://doi.org/10.1023/A:1008162829755 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 1-5 01 131-138 |
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10.1023/A:1008162829755 doi (DE-627)OLC2050511760 (DE-He213)A:1008162829755-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn Pai, Anita verfasserin aut Expanded bed adsorption on supermacroporous cross-linked cellulose matrix 1999 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Kluwer Academic Publishers 1999 Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. Gondkar, Shyamal aut Sundaram, Sumati aut Lali, Arvind aut Enthalten in Bioseparation Kluwer Academic Publishers, 1990 8(1999), 1-5 vom: Jan., Seite 131-138 (DE-627)130868930 (DE-600)1033272-8 (DE-576)063974134 0923-179X nnns volume:8 year:1999 number:1-5 month:01 pages:131-138 https://doi.org/10.1023/A:1008162829755 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4012 AR 8 1999 1-5 01 131-138 |
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expanded bed adsorption on supermacroporous cross-linked cellulose matrix |
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Expanded bed adsorption on supermacroporous cross-linked cellulose matrix |
| abstract |
Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. © Kluwer Academic Publishers 1999 |
| abstractGer |
Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. © Kluwer Academic Publishers 1999 |
| abstract_unstemmed |
Abstract Rigid spherical macroporous adsorbent beads (CELBEADS) prepared by cross-linking of cellulose were characterised and found eminently suitable for use as expanded bed affinity chromatography matrix. Chromatographic runs were performed on a 10 mm diameter column with three solutes tyrosine, papain and bovine serum albumin under non-retaining conditions on CELBEADS and $ Streamline^{TM} $ DEAE, a commercial agarose based expanded bed matrix. Performance of the runs was measured in terms of height equivalent to theoretical plate, HETP. Variation in HETP with velocity on $ Streamline^{TM} $ DEAE gave flat profiles in packed bed and increasing trend in expanded bed. On CELBEADS, the HETP curves in both packed and expanded bed modes followed profiles typical of macroporous adsorbents i.e. increasing and levelling with velocity. HETP values obtained for papain and bovine serum albumin on CELBEADS were lower than those obtained on $ Streamline^{TM} $ DEAE at all velocities. Lactate dehydrogenase was purified from porcine muscle homogenate using Cibacron blue conjugated to CELBEADS using a protocol reported for supports with surface hydroxyl groups. Elution of the enzyme was investigated both in packed mode as well as in expanded mode at a flow rate of 1 ml $ min^{-1} $. The purification procedure took about 60 minutes and a purification fold of about 14 was achieved in both cases. The adsorbent could be cleaned in place with 5 M urea and used repeatedly without loss of performance. © Kluwer Academic Publishers 1999 |
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Expanded bed adsorption on supermacroporous cross-linked cellulose matrix |
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Gondkar, Shyamal Sundaram, Sumati Lali, Arvind |
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