Evidence map›Paper›PMID 8670058›Full record

ArticleThe Biochemical journal1996

Optimized heterologous expression of the human zinc enzyme glyoxalase I.

M Ridderström, B Mannervik

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 58 citations in OpenAlex.

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  13. A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major.Proceedings of the National Academy of Sciences of the United States of America · 2004
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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

2 authors at 1 institution in 1 country.

M RidderströmDepartment of Biochemistry, Uppsala University, Biomedical Center, Sweden.
B Mannervik
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA coding for human glyoxalase I was isolated from a HeLa cell cDNA library by means of PCR. The deduced amino acid sequence differs form previously isolated sequences in that a glutamic acid replaces an alanine in position 111. This variant cDNA may represent the more acidic isoform of glyoxalase I originally identified at the protein level. An expression clone was constructed for high-level production of glyoxalase I in Escherichia coli. For optimal yield of the recombinant protein, silent random mutations were introduced in the cDNA coding region. Antisera against human glyoxalase I were used to select a high-level expression clone. This clone afforded 60 mg of purified enzyme per litre of culture medium. Addition of a zinc salt to the culture medium was essential to obtain an active enzyme and a stoicheiometric metal content. The functional characterization of the recombinant enzyme included determination of kinetic constants for methylglyoxal, phenylglyoxal and p-phenylphenylglyoxal, as well as inhibition studies. The kinetic properties of recombinant glyoxalase I were indistinguishable from those of the enzyme purified from human tissues.

Indexed as

Amino Acid SequenceBase SequenceDNA, ComplementaryHeLa CellsHumansKineticsLactoylglutathione LyaseMolecular Sequence DataRecombinant ProteinsZincDNA, ComplementaryLactoylglutathione LyaseRecombinant ProteinsZinc

Identifiers

PMID8670058
PMCPMC1217073
OpenAlexW2285485180

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.