-
Je něco špatně v tomto záznamu ?
Preparation and properties of recombinant Clostridium ramosum IgA proteinase. Isolation of Fc-SC and Fab fragments of human secretory IgA
M. Krupka, L. Raskova Kafkova, L. Barkocziova, K. Sloupenska, D. Brokesova, M. Sebela, M. Raska
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- bakteriální proteiny chemie genetika MeSH
- Firmicutes enzymologie genetika MeSH
- imunoglobulin A sekreční chemie MeSH
- imunoglobuliny - Fab fragmenty * chemie izolace a purifikace MeSH
- imunoglobuliny - Fc fragmenty * chemie izolace a purifikace MeSH
- lidé MeSH
- proteasy chemie genetika MeSH
- rekombinantní proteiny chemie genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Immunoglobulin A (IgA) proteinase from Clostridium ramosum is the enzyme which cleaves IgA of both subclasses; in contrast, the other bacterial proteinases cleave only IgA1 proteins. Previous reports characterized the activity of proteinase naturally secreted by C. ramosum specific for the normal human serum IgA of IgA1 and IgA2m(1) subclasses and also for secretory IgA (SIgA). Its amino acid sequence was determined, and the recombinant proteinase which cleaved IgA of both subclasses was prepared. Here we report the optimized expression, purification, storage conditions and activity testing against purified human milk SIgA. The recombinant C. ramosum IgA proteinase isolated in the high degree of purity exhibited almost complete cleavage of SIgA of both subclasses. The proteinase remained active upon storage for more than 10 month at -20 °C without substantial loss of enzymatic activity. Purified SIgA fragments are suitable for studies of all antigen-binding and Fc-dependent functions of SIgA involved in the protection against infections with mucosal pathogens.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc22004036
- 003
- CZ-PrNML
- 005
- 20220127145622.0
- 007
- ta
- 008
- 220113s2021 xxu f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1016/j.pep.2021.105891 $2 doi
- 035 __
- $a (PubMed)33895263
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Krupka, Michal $u Department of Immunology, Faculty of Medicine and Dentistry, Palacky University Olomouc, Olomouc, Czech Republic
- 245 10
- $a Preparation and properties of recombinant Clostridium ramosum IgA proteinase. Isolation of Fc-SC and Fab fragments of human secretory IgA / $c M. Krupka, L. Raskova Kafkova, L. Barkocziova, K. Sloupenska, D. Brokesova, M. Sebela, M. Raska
- 520 9_
- $a Immunoglobulin A (IgA) proteinase from Clostridium ramosum is the enzyme which cleaves IgA of both subclasses; in contrast, the other bacterial proteinases cleave only IgA1 proteins. Previous reports characterized the activity of proteinase naturally secreted by C. ramosum specific for the normal human serum IgA of IgA1 and IgA2m(1) subclasses and also for secretory IgA (SIgA). Its amino acid sequence was determined, and the recombinant proteinase which cleaved IgA of both subclasses was prepared. Here we report the optimized expression, purification, storage conditions and activity testing against purified human milk SIgA. The recombinant C. ramosum IgA proteinase isolated in the high degree of purity exhibited almost complete cleavage of SIgA of both subclasses. The proteinase remained active upon storage for more than 10 month at -20 °C without substantial loss of enzymatic activity. Purified SIgA fragments are suitable for studies of all antigen-binding and Fc-dependent functions of SIgA involved in the protection against infections with mucosal pathogens.
- 650 _2
- $a bakteriální proteiny $x chemie $x genetika $7 D001426
- 650 _2
- $a Firmicutes $x enzymologie $x genetika $7 D000068536
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a imunoglobulin A sekreční $x chemie $7 D007071
- 650 12
- $a imunoglobuliny - Fab fragmenty $x chemie $x izolace a purifikace $7 D007140
- 650 12
- $a imunoglobuliny - Fc fragmenty $x chemie $x izolace a purifikace $7 D007141
- 650 _2
- $a proteasy $x chemie $x genetika $7 D010447
- 650 _2
- $a rekombinantní proteiny $x chemie $x genetika $7 D011994
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Raskova Kafkova, Leona $u Department of Immunology, Faculty of Medicine and Dentistry, Palacky University Olomouc, Olomouc, Czech Republic. Electronic address: leona.raskova@upol.cz
- 700 1_
- $a Barkocziova, Lucia $u Department of Immunology, Faculty of Medicine and Dentistry, Palacky University Olomouc, Olomouc, Czech Republic
- 700 1_
- $a Sloupenska, Kristyna $u Department of Immunology, Faculty of Medicine and Dentistry, Palacky University Olomouc, Olomouc, Czech Republic
- 700 1_
- $a Brokesova, Diana $u Department of Immunology, Faculty of Medicine and Dentistry, Palacky University Olomouc, Olomouc, Czech Republic
- 700 1_
- $a Sebela, Marek $u Centre of the Region Hana for Biotechnological and Agricultural Research, Palacky University Olomouc, Olomouc, Czech Republic
- 700 1_
- $a Raska, Milan $u Department of Immunology, Faculty of Medicine and Dentistry, Palacky University Olomouc, Olomouc, Czech Republic. Electronic address: milan.raska@upol.cz
- 773 0_
- $w MED00008659 $t Protein expression and purification $x 1096-0279 $g Roč. 184, č. - (2021), s. 105891
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/33895263 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y p $z 0
- 990 __
- $a 20220113 $b ABA008
- 991 __
- $a 20220127145619 $b ABA008
- 999 __
- $a ok $b bmc $g 1751487 $s 1155185
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2021 $b 184 $c - $d 105891 $e 20210422 $i 1096-0279 $m Protein expression and purification $n Protein Expr Purif $x MED00008659
- LZP __
- $a Pubmed-20220113
