Evidence map›Paper›PMID 16788731›Full record

ArticleThe journal of medical, chemical, biological, and radiological defense2005

LARGE SCALE PURIFICATION OF BUTYRYLCHOLINESTERASE FROM HUMAN PLASMA SUITABLE FOR INJECTION INTO MONKEYS; A POTENTIAL NEW THERAPEUTIC FOR PROTECTION AGAINST COCAINE AND NERVE AGENT TOXICITY.

Oksana Lockridge, Lawrence M Schopfer, Gail Winger, James H Woods

Open access · greenAbstract read
In one paragraph

Article in The journal of medical, chemical, biological, and radiological defense, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Butyrylcholinesterase-Protein Interactions in Human Serum.International journal of molecular sciences · 2021
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Purification of recombinant human butyrylcholinesterase on Hupresin®.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Characterization of butyrylcholinesterase in bovine serum.Chemico-biological interactions · 2017
    Article
  19. Article
  20. Long-acting cocaine hydrolase for addiction therapy.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

4 authors.

Oksana Lockridge
Lawrence M Schopfer
Gail Winger
James H Woods

Funding

BCHE as a Cocaine AntagonistR01DA014023 · NIDA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WOODS, JAMES H · 2001 to 2002
$748k
NIDA NIH HHS R01 DA014023
6 · The paper itself

Abstract

Pretreatment of animals with butyrylcholinesterase (EC 3.1.1.8 BChE) provides complete protection from the acute effects of organophosphorus nerve agents. Butyrylcholinesterase has also been shown to protect from cocaine toxicity. Large amounts of highly purified butyrylcholinesterase are needed to test the effectiveness of this new therapeutic agent in monkeys. Only a minimum amount of endotoxin can be present in a therapeutic intended for injection into monkeys. Our goal was to develop a large scale purification method for human BChE from human plasma with precautions to minimize endotoxin content. A protocol was developed that processed up to 100 L of human plasma at a time. Dialysis in pH 4.0 buffer, ion exchange chromatography at pH 4, affinity chromatography on procainamide-Sepharose, and HPLC ion exchange at pH 7.4 yielded highly purified human BChE containing a low endotoxin level of about 800 EU/ml. The purified BChE produced by this method had a mean residence time of 56 h in mice and 93 h in monkeys, and caused no toxic effects. The absence of a toxic effect in monkeys demonstrates that the endotoxin level of 800 EU/ml was well tolerated by monkeys.

Identifiers

PMID16788731
PMCPMC1480358
OpenAlexW148124656

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.