Evidence map›Paper›PMID 28377345›Full record

ArticleNan fang yi ke da xue xue bao = Journal of Southern Medical University2017

[Expression of Proteus mirabilis polyphosphate kinase and preparation of its polyclonal antibodies].

Liang Peng, Jing-Yi Ou, Jia-Yun Pan, Cong Deng, Jing-Hong Chen, Hong Cao

Abstract read
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Article in Nan fang yi ke da xue xue bao = Journal of Southern Medical University, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Liang PengDepartment of Clinical Laboratory, Second Affiliated Hospital of Guangzhou Medical University, Guangzhou 510260, China.E-mail: pl_206@126.com.
Jing-Yi Ou
Jia-Yun Pan
Cong Deng
Jing-Hong Chen
Hong Cao

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveTo express and purify polyphosphate kinase (PPK) from Proteus mirabilis and prepare the polyclonal antibody against PPK.

methodsThe antigenicity and hydrophobicity of PPK were analyzed using software. The N-terminal conservative sequence containing 309 amino acids was selected as the target peptide, and its corresponding gene sequence with modification based on prokaryotic cells-preferred codon was synthesized and inserted into plasmid pET28b(+). The constructed recombinant plasmid was transformed into Escherichia coli BL21 (DE3) and induced with IPTG. The expressed fusion protein was purified using Ni-affinity chromatography. The purified protein was injected along with adjuvant in rabbits to prepare the polyclonal antibodies against PPK. RESULTS AND

conclusionPPK fusion protein expressed by E. coli was purified successfully using Ni-affinity chromatography. ELISA result demonstrated that the harvested rabbit anti-sera against PPK had a high titer of 1:512 000, and Western blotting showed a good specificity of the antibody, which can be used further study of the role of PPK in the pathogenesis of Proteus mirabilis infection.

Indexed as

AnimalsAntibodiesAntibody SpecificityBlotting, WesternEscherichia coliPhosphotransferases (Phosphate Group Acceptor)Proteus mirabilisRabbitsRecombinant Fusion ProteinsAntibodiesPhosphotransferases (Phosphate Group Acceptor)polyphosphate kinaseRecombinant Fusion Proteins

Identifiers

PMID28377345
PMCPMC6780429

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