Formation of glycoprotein degrading enzymes by Bacteroides fragilis
Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of sub...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Macfarlane, G.T. [verfasserIn] Gibson, G.R. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1991 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: FEMS microbiology letters - Federation of European Microbiological Societies ; GKD-ID: 114439X, Oxford [u.a.] : Wiley-Blackwell, 1977, 77(1991), 2/3, Seite 0 |
| Übergeordnetes Werk: |
volume:77 ; year:1991 ; number:2/3 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1111/j.1574-6968.1991.tb04363.x |
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NLEJ239732626 |
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10.1111/j.1574-6968.1991.tb04363.x doi (DE-627)NLEJ239732626 DE-627 ger DE-627 rakwb Macfarlane, G.T. verfasserin aut Formation of glycoprotein degrading enzymes by Bacteroides fragilis Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Gibson, G.R. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04363.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04363.x doi (DE-627)NLEJ239732626 DE-627 ger DE-627 rakwb Macfarlane, G.T. verfasserin aut Formation of glycoprotein degrading enzymes by Bacteroides fragilis Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Gibson, G.R. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04363.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04363.x doi (DE-627)NLEJ239732626 DE-627 ger DE-627 rakwb Macfarlane, G.T. verfasserin aut Formation of glycoprotein degrading enzymes by Bacteroides fragilis Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Gibson, G.R. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04363.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04363.x doi (DE-627)NLEJ239732626 DE-627 ger DE-627 rakwb Macfarlane, G.T. verfasserin aut Formation of glycoprotein degrading enzymes by Bacteroides fragilis Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Gibson, G.R. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04363.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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10.1111/j.1574-6968.1991.tb04363.x doi (DE-627)NLEJ239732626 DE-627 ger DE-627 rakwb Macfarlane, G.T. verfasserin aut Formation of glycoprotein degrading enzymes by Bacteroides fragilis Oxford, UK Blackwell Publishing Ltd 1991 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Gibson, G.R. verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 77(1991), 2/3, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:77 year:1991 number:2/3 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1991.tb04363.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1991 2/3 0 |
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Formation of glycoprotein degrading enzymes by Bacteroides fragilis |
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Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. |
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Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. |
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Bacteroides fragilis NCDO 2217 produced a wide range of cell-associated hydrolytic enzymes (neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase, β-galactosidase, β-N-acetylglucosaminidase) that could potentially degrade the carbohydrate moieties of mucin, a complex glycoprotein. The type of substrate used for growth markedly influenced their formation in batch cultures. Synthesis of neuraminidase, α-fucosidase, α-N-acetylgalactosaminidase and to a lesser extent, β-N-acetylglucosaminidase, was inversely related to growth rate in continuous cultures (D= 0.03 h−1– 0.23 h−1) in which porcine gastric mucin provided the sole source of carbon and nitrogen. |
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7.399987 |