One-step FPLC-size-exclusion chromatography procedure for purification of rDMBT1 6 kb with increased biological activity.

Pernille Lund Hansen

doi:10.1016/j.ab.2017.11.015

One-step FPLC-size-exclusion chromatography procedure for purification of rDMBT1 6 kb with increased biological activity.

Bidragets oversatte titel: Et-trins kromatografi FPLC procedure til oprensning af rekombinant DMBT1 6 kb med øget biologisk aktivitet

Pernille Lund Hansen

Syddansk Universitet

Publikation: Bidrag til tidsskrift › Tidsskriftsartikel › Forskning › peer review

Abstract

Deleted in Malignant Brain Tumor 1 (DMBT1, alias SAG or gp340) is a pattern recognition receptor involved in immune defense, cell polarization, differentiation and regeneration. To investigate the role of the protein in physiological and pathological processes, the protein has often been isolated from saliva or produced in vitro and purified by a multistep affinity purification procedure using bacteria, followed by FPLC. Here, we compared a simple, one-step FPLC-SEC protocol for purification of recombinant DMBT1 6 kb, with that of the standard bacteria affinity purification-based protocol. Our data suggest that our FPLC-SEC protocol yields DMBT1 in a more native conformation.

Bidragets oversatte titel	Et-trins kromatografi FPLC procedure til oprensning af rekombinant DMBT1 6 kb med øget biologisk aktivitet
Originalsprog	Engelsk
Tidsskrift	Analytical Biochemistry
ISSN	0003-2697
DOI	https://doi.org/10.1016/j.ab.2017.11.015
Status	Udgivet - 21 nov. 2017
Udgivet eksternt	Ja

Adgang til dokumentet

10.1016/j.ab.2017.11.015

https://www.sciencedirect.com/science/article/pii/S0003269717304621?via%3Dihub

Andre filer og links

https://doi.org/10.1016/j.ab.2017.11.015

Citationsformater

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abstract = "Deleted in Malignant Brain Tumor 1 (DMBT1, alias SAG or gp340) is a pattern recognition receptor involved in immune defense, cell polarization, differentiation and regeneration. To investigate the role of the protein in physiological and pathological processes, the protein has often been isolated from saliva or produced in vitro and purified by a multistep affinity purification procedure using bacteria, followed by FPLC. Here, we compared a simple, one-step FPLC-SEC protocol for purification of recombinant DMBT1 6 kb, with that of the standard bacteria affinity purification-based protocol. Our data suggest that our FPLC-SEC protocol yields DMBT1 in a more native conformation.",

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N2 - Deleted in Malignant Brain Tumor 1 (DMBT1, alias SAG or gp340) is a pattern recognition receptor involved in immune defense, cell polarization, differentiation and regeneration. To investigate the role of the protein in physiological and pathological processes, the protein has often been isolated from saliva or produced in vitro and purified by a multistep affinity purification procedure using bacteria, followed by FPLC. Here, we compared a simple, one-step FPLC-SEC protocol for purification of recombinant DMBT1 6 kb, with that of the standard bacteria affinity purification-based protocol. Our data suggest that our FPLC-SEC protocol yields DMBT1 in a more native conformation.

AB - Deleted in Malignant Brain Tumor 1 (DMBT1, alias SAG or gp340) is a pattern recognition receptor involved in immune defense, cell polarization, differentiation and regeneration. To investigate the role of the protein in physiological and pathological processes, the protein has often been isolated from saliva or produced in vitro and purified by a multistep affinity purification procedure using bacteria, followed by FPLC. Here, we compared a simple, one-step FPLC-SEC protocol for purification of recombinant DMBT1 6 kb, with that of the standard bacteria affinity purification-based protocol. Our data suggest that our FPLC-SEC protocol yields DMBT1 in a more native conformation.

UR - https://doi.org/10.1016/j.ab.2017.11.015

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DO - 10.1016/j.ab.2017.11.015

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SN - 0003-2697

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JF - Analytical Biochemistry

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