Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase
Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Sato, Nobuyuki [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1994 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 1994 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 41(1994), 1 vom: März, Seite 39-46 |
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| Übergeordnetes Werk: |
volume:41 ; year:1994 ; number:1 ; month:03 ; pages:39-46 |
| Links: |
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| DOI / URN: |
10.1007/BF00166079 |
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| 245 | 1 | 0 | |a Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase |
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| 520 | |a Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. | ||
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| 700 | 1 | |a Shimada, Masahiko |4 aut | |
| 700 | 1 | |a Nakajima, Hiroshi |4 aut | |
| 700 | 1 | |a Oda, Hiroshi |4 aut | |
| 700 | 1 | |a Kimura, Shoji |4 aut | |
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10.1007/BF00166079 doi (DE-627)OLC2050671504 (DE-He213)BF00166079-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. Enzyme Peptide Codon Carbon Source Molecular Mass Shimada, Masahiko aut Nakajima, Hiroshi aut Oda, Hiroshi aut Kimura, Shoji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 41(1994), 1 vom: März, Seite 39-46 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:41 year:1994 number:1 month:03 pages:39-46 https://doi.org/10.1007/BF00166079 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 41 1994 1 03 39-46 |
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10.1007/BF00166079 doi (DE-627)OLC2050671504 (DE-He213)BF00166079-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. Enzyme Peptide Codon Carbon Source Molecular Mass Shimada, Masahiko aut Nakajima, Hiroshi aut Oda, Hiroshi aut Kimura, Shoji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 41(1994), 1 vom: März, Seite 39-46 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:41 year:1994 number:1 month:03 pages:39-46 https://doi.org/10.1007/BF00166079 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 41 1994 1 03 39-46 |
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10.1007/BF00166079 doi (DE-627)OLC2050671504 (DE-He213)BF00166079-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. Enzyme Peptide Codon Carbon Source Molecular Mass Shimada, Masahiko aut Nakajima, Hiroshi aut Oda, Hiroshi aut Kimura, Shoji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 41(1994), 1 vom: März, Seite 39-46 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:41 year:1994 number:1 month:03 pages:39-46 https://doi.org/10.1007/BF00166079 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 41 1994 1 03 39-46 |
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10.1007/BF00166079 doi (DE-627)OLC2050671504 (DE-He213)BF00166079-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. Enzyme Peptide Codon Carbon Source Molecular Mass Shimada, Masahiko aut Nakajima, Hiroshi aut Oda, Hiroshi aut Kimura, Shoji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 41(1994), 1 vom: März, Seite 39-46 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:41 year:1994 number:1 month:03 pages:39-46 https://doi.org/10.1007/BF00166079 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 41 1994 1 03 39-46 |
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10.1007/BF00166079 doi (DE-627)OLC2050671504 (DE-He213)BF00166079-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Sato, Nobuyuki verfasserin aut Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. Enzyme Peptide Codon Carbon Source Molecular Mass Shimada, Masahiko aut Nakajima, Hiroshi aut Oda, Hiroshi aut Kimura, Shoji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 41(1994), 1 vom: März, Seite 39-46 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:41 year:1994 number:1 month:03 pages:39-46 https://doi.org/10.1007/BF00166079 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 41 1994 1 03 39-46 |
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Enthalten in Applied microbiology and biotechnology 41(1994), 1 vom: März, Seite 39-46 volume:41 year:1994 number:1 month:03 pages:39-46 |
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Enthalten in Applied microbiology and biotechnology 41(1994), 1 vom: März, Seite 39-46 volume:41 year:1994 number:1 month:03 pages:39-46 |
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Sato, Nobuyuki @@aut@@ Shimada, Masahiko @@aut@@ Nakajima, Hiroshi @@aut@@ Oda, Hiroshi @@aut@@ Kimura, Shoji @@aut@@ |
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Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase |
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Sato, Nobuyuki Shimada, Masahiko Nakajima, Hiroshi Oda, Hiroshi Kimura, Shoji |
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cloning and expression in escherichia coli of the gene encoding the proteus vulgaris chondroitin abc lyase |
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Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase |
| abstract |
Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. © Springer-Verlag 1994 |
| abstractGer |
Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. © Springer-Verlag 1994 |
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Abstract The structural gene encoding chondroitin ABC lyase from Proteus vulgaris was cloned and sequenced. This gene consists of a single open reading frame of 3,063 bp, including a sequence (72 bp) for a possible secretory protein leader peptide, preceded by a Shire-Dalgarno ribosomal binding site. Promoter-like and ϱ-independent terminator sequences were detected upstream and downstream of the open reading frame, respectively. The G + C content of the coding region was 38.6%. The transcription startpoint was located 41-bp upstream of the initiation codon (ATG). Chondroitin ABC lyase is composed of 997 amino acids, ans a relative molecular mass of 112,635. When the 5.2-kb fragment containing the 1.2-kb upstream from the gene was inserted into pSTV29, and cloned in Escherichia coli, chondroitin ABC lyase was induced in the medium containing chondroitin-6-sulfate as the carbon source. On the other hand, when a 4.2-kb fragment containing only 0.2 kb upstream was inserted into pSTV29(pCHSΔ6), and pCHSΔ6 was introduced into E. coli, the enzyme was constitutively produced, even in medium containing glucose as the carbon source. By immunoblot analysis, the polypeptide synthesized by E. coli cells carrying pCHSΔ6 appeared to be the same as that of the purified chonditin ABC lyase from P. vulgaris. © Springer-Verlag 1994 |
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