Abstract:
:The Staphylococcus aureus protein A (SpA) can be obtained through the culture of wild-type S. aureus and also as a recombinant protein in safe bacterial hosts. Several methods have been used to purify SpA among which ion-exchange chromatography, affinity chromatography, gel filtration, and per aqueous liquid chromatography (PALC) are common. SpA has a wide range of biochemical, biotechnological, and medical applications and is most commonly used in test methods such as immunoprecipitation, enzyme-linked immunosorbent assay, and Western blotting. SpA has also been widely utilized in pharmaceutical applications to bind to immune complexes and serum immunoglobulins. SpA also directly binds to the B-cells preventing initiation of infectious diseases as well as having a role in the development of various autoimmune diseases. This review considers different applications of SpA in biotechnology and its novel clinical application for effective treatment of autoimmune diseases. It also discusses various strategies for expression and purification of the SpA including types of column chromatography that are commonly used in protein purification and developing SpA surface display technologies. Finally, this review highlights the potential and novel applications of SpA immobilization, SpA typing, protein engineering for further development of immunological and biochemical research, and also application of SpA as a diagnostic biosensor.
journal_name
Biotechnol Appl Biochemjournal_title
Biotechnology and applied biochemistryauthors
Rigi G,Ghaedmohammadi S,Ahmadian Gdoi
10.1002/bab.1742subject
Has Abstractpub_date
2019-05-01 00:00:00pages
454-464issue
3eissn
0885-4513issn
1470-8744journal_volume
66pub_type
杂志文章,评审abstract::A chitin-degrading Bacillus strain, designated as NCTU2, was screened from soil and identified. An extracellular chitinase was purified to >90% homogeneity from the culture filtrate. The purification involved hydrophobic-interaction and gel-filtration chromatographic separations with a yield of 58%. The purified enzym...
journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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更新日期:1992-08-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
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doi:
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
pub_type: 杂志文章
doi:
更新日期:1994-10-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
pub_type: 杂志文章
doi:
更新日期:1991-04-01 00:00:00
abstract::Two different enzymes that metabolize lactate in the presence of oxygen, either to acetate plus CO2 (lactate 2-mono-oxygenase; Lmox) or to pyruvate plus H2O2 (lactate oxidase; Lox) were encapsulated in human and murine red blood cells (RBCs). Lmox shows a low affinity for lactate (Km 22 mM) and thus works at a low rat...
journal_title:Biotechnology and applied biochemistry
pub_type: 杂志文章
doi:
更新日期:1995-12-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
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更新日期:1990-10-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
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更新日期:2015-11-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
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更新日期:1999-02-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
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更新日期:1991-10-01 00:00:00
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更新日期:2007-05-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
pub_type: 杂志文章
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更新日期:1988-10-01 00:00:00