Recombinant α-NAcetylgalactosaminidase from Marine Bacterium-Modifying A Erythrocyte Antigens.

L A Balabanova, V A Golotin, I Y Bakunina, L V Slepchenko, V V Isakov, A B Podvolotskaya, V A Rasskazov

Open access · bronzeAbstract read

In one paragraph

Article in Acta naturae. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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0cells of the map it votes in

2citing papers in PubMed

–field-weighted citation impact, top 100% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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, 5 citations in OpenAlex.

Prospecting for microbial α-The Journal of biological chemistry · 2019
Article
Effect of Pentacyclic Guanidine Alkaloids from the SpongeMarine drugs · 2019
Article

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

7 authors at 2 institutions in 1 country.

L A BalabanovaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 100-letiya Vladivostoka Ave., 159, 690022, Vladivostok, Russia ; Far Eastern Federal University, Sukhanova Str., 8, 690950, Vladivostok, Russia.

V A GolotinG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 100-letiya Vladivostoka Ave., 159, 690022, Vladivostok, Russia.

I Y BakuninaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 100-letiya Vladivostoka Ave., 159, 690022, Vladivostok, Russia.

L V SlepchenkoG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 100-letiya Vladivostoka Ave., 159, 690022, Vladivostok, Russia.

V V IsakovG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 100-letiya Vladivostoka Ave., 159, 690022, Vladivostok, Russia.

A B PodvolotskayaFar Eastern Federal University, Sukhanova Str., 8, 690950, Vladivostok, Russia.

V A RasskazovFar Eastern Federal University, Sukhanova Str., 8, 690950, Vladivostok, Russia.

Pacific Institute of Bioorganic Chemistry. GB Elyakova Far Eastern Branch of the Russian Academy of Sciences · RUFar Eastern Federal University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A plasmid based on pET-40b was constructed to synthesize recombinant α-N-acetylgalactosaminidase of the marine bacterium Arenibacter latericius KMM 426T (α-AlNaGal) in Escherichia coli cells. The yield of α-Al- NaGal attains 10 mg/ml with activity of 49.7 ± 1.3 U at 16°C, concentration of inductor 2 mM, and cultivation for 12 h. Techniques such as anion exchange, metal affinity and gel filtration chromatography to purify α-AlNaGal were applied. α-AlNaGal is a homodimer with a molecular weight of 164 kDa. This enzyme is stable at up to 50°C with a temperature range optimum activity of 20-37°C. Furthermore, its activity is independent of the presence of metal ions in the incubation medium. 1H NMR spectroscopy revealed that α-AlNaGal catalyzes the hydrolysis of the O-glycosidic bond with retention of anomeric stereochemistry and possesses a mechanism of action identical to that of other glycoside hydrolases of the 109 family. α-AlNaGal reduces the serological activity of A erythrocytes at pH 7.3. This property of α-AlNaGal can potentially be used for enzymatic conversion of A and AB erythrocytes to blood group O erythrocytes.

Indexed as

1H NMR spectroscopyArenibacter latericiusconversion of A erythrocytesglycoside hydrolase GH109

Identifiers

PMID25927009

PMCPMC4410403

OpenAlexW324931465

What OpenQuestion holds

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LicenceCC BY

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.