Improved method for expression and isolation of the Mycoplasma hominis arginine deiminase from the recombinant strain of Escherichia coli.
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| Title: | Improved method for expression and isolation of the Mycoplasma hominis arginine deiminase from the recombinant strain of Escherichia coli. |
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| Authors: | Fayura, Lyubov R.1, Boretsky, Yuriy R.1, Pynyaha, Yuriy V.1, Wheatley, Denys N.2, Sibirny, Andriy A.1,3 sibirny@cellbiol.lviv.ua |
| Source: | Journal of Biotechnology. Sep2013, Vol. 167 Issue 4, p420-426. 7p. |
| Subjects: | Mycoplasma, Arginine deiminase, Gene expression, Chemical reagents, Bacterial genetics, Cost effectiveness, Escherichia coli |
| Abstract: | Highlights: [•] M. hominis gene coding for arginine deiminase was cloned and expressed successfully. [•] The recombinant arginine deiminase producer is stabilized significantly. [•] The expensive reagents are substituted with cheaper ones. [•] The expressed protein has been purified successfully. [•] As a result low-cost method for high-efficient production of arginine deiminase is developed. [ABSTRACT FROM AUTHOR] |
| 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: 90302521 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Improved method for expression and isolation of the Mycoplasma hominis arginine deiminase from the recombinant strain of Escherichia coli. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Fayura%2C+Lyubov+R%2E%22">Fayura, Lyubov R.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Boretsky%2C+Yuriy+R%2E%22">Boretsky, Yuriy R.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Pynyaha%2C+Yuriy+V%2E%22">Pynyaha, Yuriy V.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Wheatley%2C+Denys+N%2E%22">Wheatley, Denys N.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Sibirny%2C+Andriy+A%2E%22">Sibirny, Andriy A.</searchLink><relatesTo>1,3</relatesTo><i> sibirny@cellbiol.lviv.ua</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Biotechnology%22">Journal of Biotechnology</searchLink>. Sep2013, Vol. 167 Issue 4, p420-426. 7p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Mycoplasma%22">Mycoplasma</searchLink><br /><searchLink fieldCode="DE" term="%22Arginine+deiminase%22">Arginine deiminase</searchLink><br /><searchLink fieldCode="DE" term="%22Gene+expression%22">Gene expression</searchLink><br /><searchLink fieldCode="DE" term="%22Chemical+reagents%22">Chemical reagents</searchLink><br /><searchLink fieldCode="DE" term="%22Bacterial+genetics%22">Bacterial genetics</searchLink><br /><searchLink fieldCode="DE" term="%22Cost+effectiveness%22">Cost effectiveness</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Highlights: [•] M. hominis gene coding for arginine deiminase was cloned and expressed successfully. [•] The recombinant arginine deiminase producer is stabilized significantly. [•] The expensive reagents are substituted with cheaper ones. [•] The expressed protein has been purified successfully. [•] As a result low-cost method for high-efficient production of arginine deiminase is developed. [ABSTRACT FROM AUTHOR] – 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.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.jbiotec.2013.06.025 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 7 StartPage: 420 Subjects: – SubjectFull: Mycoplasma Type: general – SubjectFull: Arginine deiminase Type: general – SubjectFull: Gene expression Type: general – SubjectFull: Chemical reagents Type: general – SubjectFull: Bacterial genetics Type: general – SubjectFull: Cost effectiveness Type: general – SubjectFull: Escherichia coli Type: general Titles: – TitleFull: Improved method for expression and isolation of the Mycoplasma hominis arginine deiminase from the recombinant strain of Escherichia coli. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Fayura, Lyubov R. – PersonEntity: Name: NameFull: Boretsky, Yuriy R. – PersonEntity: Name: NameFull: Pynyaha, Yuriy V. – PersonEntity: Name: NameFull: Wheatley, Denys N. – PersonEntity: Name: NameFull: Sibirny, Andriy A. IsPartOfRelationships: – BibEntity: Dates: – D: 20 M: 09 Text: Sep2013 Type: published Y: 2013 Identifiers: – Type: issn-print Value: 01681656 Numbering: – Type: volume Value: 167 – Type: issue Value: 4 Titles: – TitleFull: Journal of Biotechnology Type: main |
| ResultId | 1 |