Vibrio cholerae periplasmic superoxide dismutase: isolation of the gene and overexpression of the protein
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| Title: | Vibrio cholerae periplasmic superoxide dismutase: isolation of the gene and overexpression of the protein |
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| Authors: | Gabbianelli, R.1 roberta.gabbianelli@iss.it, Signoretti, C.1, Marta, I.1, Battistoni, A.2, Nicolini, L.1 |
| Source: | Journal of Biotechnology. Apr2004, Vol. 109 Issue 1/2, p123. 8p. |
| Subjects: | Superoxide dismutase, Immune system, Pathogenic microorganisms, Vibrio cholerae |
| Abstract: | Superoxide dismutases are ubiquitous enzymes which play an important role in protecting cells against oxidative damage and which have also been shown to contribute to the pathogenicity of many bacterial species. Here we demonstrate that Vibrio cholerae, the causative agent of cholerae, expresses an active periplasmic Cu,Zn superoxide dismutase. Moreover, we have set up an expression system yielding large amounts of V. cholerae recombinant Cu,Zn superoxide dismutase in the periplasm of Escherichia coli and a procedure to obtain the enzyme in a highly purified form. Unlike the bovine enzyme, V. cholerae Cu,Zn superoxide dismutase has been proved to be highly resistant to inactivation by hydrogen peroxide. This property, which appears to be common to other bacterial enzymes of this class, might improve the ability of Cu,Zn superoxide dismutase to protect bacteria against the reactive oxygen species produced by phagocytes. [Copyright &y& Elsevier] |
| Copyright of Journal of Biotechnology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 12741430 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Vibrio cholerae periplasmic superoxide dismutase: isolation of the gene and overexpression of the protein – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Gabbianelli%2C+R%2E%22">Gabbianelli, R.</searchLink><relatesTo>1</relatesTo><i> roberta.gabbianelli@iss.it</i><br /><searchLink fieldCode="AR" term="%22Signoretti%2C+C%2E%22">Signoretti, C.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Marta%2C+I%2E%22">Marta, I.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Battistoni%2C+A%2E%22">Battistoni, A.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Nicolini%2C+L%2E%22">Nicolini, L.</searchLink><relatesTo>1</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Biotechnology%22">Journal of Biotechnology</searchLink>. Apr2004, Vol. 109 Issue 1/2, p123. 8p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Superoxide+dismutase%22">Superoxide dismutase</searchLink><br /><searchLink fieldCode="DE" term="%22Immune+system%22">Immune system</searchLink><br /><searchLink fieldCode="DE" term="%22Pathogenic+microorganisms%22">Pathogenic microorganisms</searchLink><br /><searchLink fieldCode="DE" term="%22Vibrio+cholerae%22">Vibrio cholerae</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Superoxide dismutases are ubiquitous enzymes which play an important role in protecting cells against oxidative damage and which have also been shown to contribute to the pathogenicity of many bacterial species. Here we demonstrate that Vibrio cholerae, the causative agent of cholerae, expresses an active periplasmic Cu,Zn superoxide dismutase. Moreover, we have set up an expression system yielding large amounts of V. cholerae recombinant Cu,Zn superoxide dismutase in the periplasm of Escherichia coli and a procedure to obtain the enzyme in a highly purified form. Unlike the bovine enzyme, V. cholerae Cu,Zn superoxide dismutase has been proved to be highly resistant to inactivation by hydrogen peroxide. This property, which appears to be common to other bacterial enzymes of this class, might improve the ability of Cu,Zn superoxide dismutase to protect bacteria against the reactive oxygen species produced by phagocytes. [Copyright &y& Elsevier] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Biotechnology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=12741430 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.jbiotec.2004.01.002 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 123 Subjects: – SubjectFull: Superoxide dismutase Type: general – SubjectFull: Immune system Type: general – SubjectFull: Pathogenic microorganisms Type: general – SubjectFull: Vibrio cholerae Type: general Titles: – TitleFull: Vibrio cholerae periplasmic superoxide dismutase: isolation of the gene and overexpression of the protein Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Gabbianelli, R. – PersonEntity: Name: NameFull: Signoretti, C. – PersonEntity: Name: NameFull: Marta, I. – PersonEntity: Name: NameFull: Battistoni, A. – PersonEntity: Name: NameFull: Nicolini, L. IsPartOfRelationships: – BibEntity: Dates: – D: 08 M: 04 Text: Apr2004 Type: published Y: 2004 Identifiers: – Type: issn-print Value: 01681656 Numbering: – Type: volume Value: 109 – Type: issue Value: 1/2 Titles: – TitleFull: Journal of Biotechnology Type: main |
| ResultId | 1 |